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The delaying of absorption of glucose is one of the principal therapeutic approaches of type 2 diabetes. α-glucosidase inhibitors compete with the α-glucosidase enzyme activity, which helps to reduce the conversion of carbohydrates into glucose and thereby control the postprandial hyperglycemia incidence.The aim of this study was to synthesize a series of novel 1,5-diphenyl pyrrole derivatives and evaluate their in vitro α-glucosidase inhibitory activities.Compounds were synthesized through a multistep reaction and were evaluated for α- glucosidase inhibitory activities. Molecular docking and kinetic studies were carried out to predict the mode of binding and mechanism of inhibition for the most active compounds, 5g and 5b, against α-glucosidase.Synthesized compounds showed good in vitro α-glucosidase inhibitory activity with ICThe results of our study revealed that the synthesized compounds are a potential candidate for α-glucosidase inhibitors for the management of postprandial hyperglycemia for further investigation.

Ketoconazole is an imidazole fungicide which is commonly used as pharmaceutical and healthcare products. Residual amount of this compound can cause adverse ecological health problems. The present study investigated ketoconazole photocatalytic degradation using Ag

Background: Delaying the absorption of glucose through α-glucosidase enzyme inhibition is one of the therapeutic approaches in the management of Type 2 diabetes, which can reduce the incidence of postprandial hyperglycemia. The existence of chronic postprandial hyperglycemia impaired the endogenous antioxidant defense by inducing oxidative stress-induced pancreatic β-cell destruction through uncontrolled generation of free radicals such as ROS, which in turn, leads to various macrovascular and microvascular complications. The currently available α -glucosidase inhibitors, for instance, acarbose, have some side effects such as hypoglycemia at higher doses, liver problems, meteorism, diarrhea, and lactic acidosis. Therefore, there is an urgent need to discover and develop potential α-glucosidase inhibitors. Objective: Based on suchmotifs, researchers are intrigued to search for the best scaffold that displays various biological activities. Among them, coumarin scaffold has attracted great attention. The compound and its derivatives can be isolated from various natural products and/or synthesized for the development of novel α-glucosidase inhibitors. Results: This study focused on coumarin and its derivatives as well as on their application as potent antidiabetic agents and has also concentrated on the structure-activity relationship. Conclusion: This review describes the applications of coumarin-containing derivatives as α - glucosidase inhibitors based on published reports which will be useful for innovative approaches in the search for novel coumarin-based antidiabetic drugs with less toxicity and more potency.

In this work, new derivatives of diarylimidazole-1,2,3-triazole 7a-p were designed, synthesized, and evaluated for their in vitro α-glucosidase inhibitory activity. All compounds showed potent inhibitory activity in the range of IC50 = 90.4–246.7 µM comparing with acarbose as the standard drug (IC50 = 750.0 µM). Among the synthesized compounds, compounds 7b, 7c, and 7e were approximately 8 times more potent than acarbose. The kinetic study of those compounds indicated that they acted as the competitive inhibitors of α-glucosidase. Molecular docking studies were also carried out for compounds 7b, 7c, and 7e using modeled α-glucosidase to find the interaction modes responsible for the desired inhibitory activity.

Fourteen novel 4,5-diphenyl-imidazol-1,2,3-triazole hybrids 8a–n were synthesized with good yields by performing click reaction between the 4,5-diphenyl-2-(prop-2-yn-1-ylthio)-1H-imidazole and various benzyl azides. The synthesized compounds 8a–n were evaluated against yeast α-glucosidase, and all these compounds exhibited excellent inhibitory activity (IC50 values in the range of 85.6 ± 0.4–231.4 ± 1.0 μM), even much more potent than standard drug acarbose (IC50 = 750.0 μM). Among them, 4,5-diphenyl-imidazol-1,2,3-triazoles possessing 2-chloro and 2-bromo-benzyl moieties (compounds 8g and 8i) demonstrated the most potent inhibitory activities toward α-glucosidase. The kinetic study of the compound 8g revealed that this compound inhibited α-glucosidase in a competitive mode. Furthermore, docking calculations of these compounds were performed to predict the interaction mode of the synthesized compounds in the active site of α-glucosidase. A novel series of 4,5-diphenyl-imidazol-1,2,3-triazole hybrids 8a–n was synthesized with good yields by performing click reaction between the 4,5-diphenyl-2-(prop-2-yn-1-ylthio)-1Himidazole and various benzyl azides. The synthesized compounds 8a–n were evaluated against yeast α-glucosidase and all these compounds exhibited excellent inhibitory activity (IC50 values in the range of 85.6 ± 0.4-231.4 ± 1.0 μM), even much more potent than standard drug acarbose (IC50 = 750.0 μM).

Bacterial inulinases are the key enzymes in the enzymatic hydrolysis of inulin and production of fructooligosaccharides (FOSs) and high fructose syrup (HFS). An extremophilic inulinase was purified from Alkalibacillus filiformis using 80% ethanol precipitation, ultrafiltration, and Q-Sepharose anion exchange chromatography. The purified inulinase was highly active in a wide range of pH, temperature, chemical reagents, and NaCl concentrations. The enzyme immobilization on cobalt ferrite magnetic nanoparticles (CoFe 2 O 4 MNPs) was carried out by carrier binding method with covalent linkage and showed improved stability and reusability within a broad temperature and pH range, compared with the free enzyme. Using free and immobilized inulinases from A. filiformis , 122 g L −1 and 160 g L −1 fructose with 61% and 80% conversion, respectively, were obtained, with inulin as the substrate. The enzymatic properties, such as notable stability under extreme conditions, make the inulinase from A. filiformis a promising candidate for related biotechnological applications.

Laccase mediated bio-delignification has shown promising results for the removal of lignin from bio-wastes and for providing a sustainable future for using of lignocellulosic materials in different industries. This study reports an extracellular laccase from Lentinus tigrinus with delignification capability. The production of laccase was enhanced through a solid-state fermentation on the pistachio shell bio-waste to 172.0 U mg−1 (8.2-fold) by one-factor-at-a-time optimizing of fermentation conditions. Laccase was purified using a new synthetic affinity resin yielding a specific activity of 543.6 U mg−1 and a 23.9-fold purification. The purified laccase was then immobilized covalently on the large pore magnetic SBA-15. Compared to free enzyme, immobilized enzyme maintained more stable at pH 2.0–11.0 and 25–55 °C, and against organic solvents, surfactants, metal ions, and inhibitors. The activity of both forms of the enzyme was increased with Cu2+, Ca+2, cetyltrimethylammonium bromide, and ethyl acetate. A 0.72 V redox potential caused enzyme specificity to various substrates. 80% of lignin content of the bio-waste was removed by 50 U mL−1 of immobilized enzyme after 8 h fermentation and delignification efficiency was greatly increased by applying higher enzyme dosages, surfactants, and organic solvents. In addition, residual activity was more than 50% after 20 cycles of delignification. The results of delignification were confirmed by GC-MS, SEM, and composition analysis of pistachio shells. This study illustrated the notable promise of the enzyme for biotechnological and environmental applications.

A series of new Schiff bases bearing 1,2,3-triazole 12a-o was designed, synthesized, and evaluated as α-glucosidase inhibitors. All the synthesized compounds showed promising inhibition against α-glucosidase and were more potent than the standard drug acarbose. The kinetic study on the most potent compound 12n showed that this compound acted as a competitive α-glucosidase inhibitor. The docking study revealed that the synthesized compounds interacted with the important residues in the active site of α-glucosidase.

A heterogeneous biocatalyst composed of laccase immobilized on Fe3O4 magnetic nanoparticles was prepared via a click chemistry reaction for dimerization of phenylacetylene. The physical and chemical characteristics of the catalyst were investigated. Yield and efficiency of immobilization were 68.7% and 76.4%, respectively. The apparent Km value of the immobilized laccase on nanoparticles was 1.5-fold greater than the value of the free enzyme, and the calculated Vmax of free and immobilized laccase was 65 mM min‒1 and 43 mM min‒1, respectively. While the free enzyme completely lost its activity, more than 60% of the initial activity of immobilized laccase was conserved after 30 days. Oxidative dimerization of phenylacetylene was performed using the prepared catalyst and 2,2,6,6-tetramethylpiperidine1-oxyl (TEMPO) as a mediator. The maximum yield was obtained at optimal conditions: immobilized laccase (100 mg, ∼80 U), TEMPO (4 mol%), 40 °C, pH 4.5, and 6 h incubation time. Additional environmental and eco-friendly aspects of this heterogeneous biocatalyst are its potential catalytic activity and ease of separation of the catalyst from the reaction mixture by an external magnetic field. HighlightsA heterogeneous biocatalyst was prepared by immobilization of laccase on Fe3O4 nanoparticles.6-Hepynoic acid was used as a linker via a click reaction.The heterogeneous biocatalyst was used in dimerization of phenylacetylene.A maximal yield was obtained after a 6 h-incubation at 40 °C and a pH of 4.5.The catalyst was reused up to 15 runs with more than 80% conversion. A heterogeneous biocatalyst was prepared by immobilization of laccase on Fe3O4 nanoparticles. 6-Hepynoic acid was used as a linker via a click reaction. The heterogeneous biocatalyst was used in dimerization of phenylacetylene. A maximal yield was obtained after a 6 h-incubation at 40 °C and a pH of 4.5. The catalyst was reused up to 15 runs with more than 80% conversion.

Owing to their superior catalytic activity in the extreme conditions, extremozymes have found the potential biotechnological applications for industrial purposes. A robust extracellular protease activity was detected in the culture broth of

Antibody-drug conjugates are now of considerable interest and are recommended for the treatment of cancers. Linkers are having a crucial role in potency and efficacy of these drugs. Herein, for the first time, we have used a water-soluble poly-ethylene glycol based linker (succinimidyl-[(N-maleimido propionamido)-diethyleneglycol] [SM(PEG)2]) for lysine amide coupling of DM1 drug to trastuzumab considering evaluation of the effect of using a hydrophilic linker on physicochemical and biological properties of the resulting conjugate in comparison to the conjugate containing succinimidyl 4-(N-maleimidomethyl) cyclohexane-1-carboxylate (SMCC) linker, which has a relative hydrophobic nature. The physicochemical properties of synthesized conjugates were investigated in terms of drug to antibody ratio, size variants and free drug quantities. In vitro biological activity of trastuzumab-DM1 conjugates was assessed on breast cancer cell lines expressing different levels of HER2 using binding affinity, antiproliferative, apoptosis, and antibody-dependent cell-mediated cytotoxicity (ADCC) assays. Synthesized conjugate containing hydrophilic linker, showed higher drug to antibody ratio, no aggregated form and higher cellular toxicity in comparison to SMCC bearing conjugate. Binding affinity and ADCC potential of conjugates was not affected upon the usage of hydrophilic linker. In conclusion, application of SM(PEG)2 for coupling of DM1 to trastuzumab enhance desirable characteristics of the resulting conjugate.

In this study, we reported the discovery of pyridazine based 1,2,3-triazole derivatives as inhibitors of α-glucosidase. All target compounds exhibited significant inhibitory activities against yeast and rat α-glucosidase enzymes compared to positive control, acarbose. The most potent compound 6j, ethyl 3-(2-(1-(4-nitrobenzyl)-1H-1,2,3-triazol-4-yl)ethyl)-5,6-diphenylpyridazine-4-carboxylate exhibited IC50 values of 58, and 73 µM. Docking studies indicated the responsibility of hydrophobic and hydrogen bonding interactions in the ligand-enzyme complex stability. The in-vitro safety against the normal cell line was observed by toxicity evaluation of the selected compounds.

In this study, new tri-amides 5a-l have been synthesized via a one-pot four-component Ugi reaction between repaglinide, aniline derivatives, aldehyde derivatives, and cyclohexyl isocyanide in good yields. These compounds were evaluated against yeast α-glucosidase. Obtained in vitro α-glucosidase results demonstrated that all the synthesized compounds 5a-l were more potent than standard inhibitor acarbose. Among them, the most potent compounds were compounds 5j, 5k, and 5h. The kinetic analysis of the most potent compound 5j revealed that this compound is a competitive inhibitor for α-glucosidase (Ki = 24 µM). Furthermore, docking study of the most potent compounds was also performed in the α-glucosidase active site to find interaction modes and binding energies of these compounds.

Fucoxanthin is a bioactive carotenoid, found in algal species. The marine microalga Tisochrysis lutea is an interesting source of nutrients and valuable compounds like fucoxanthin. In the present work, the response surface methodology was applied to optimize the culture media in order to achieve high level of fucoxanthin from the T. lutea cultivated in 1-L batch photo-bioreactors. The relationship between fucoxanthin production and the culture medium parameters was fitted with a second-order polynomial equation using a multiple regression technique from the experimental results of the response surface methodology. The optimum composition required to obtain the highest amount of fucoxanthin was determined as follows: salinity, 36.27 g L−1; carbon source (starch), 3.90 g L−1; nitrogen source (nitrate), 0.162 g L−1. Optimum conditions significantly enhance the production of fucoxanthin (79.40 ± 0.95 mg g−1 dry weight) and decrease the period of cultivation from 14 days (in non-optimized conditions) to 4 days.

Eighteen dihydroindolizino[8,7-b]indole derivatives 4a–r were designed, synthesized and evaluated as new α-glucosidase inhibitors. These derivatives were synthesized by an efficient one-pot two-step reaction under mild condition. All the synthesized compounds were found to be more active than the standard drug acarbose (IC50 = 750.0 ± 1.5 µM) with IC50 values in the range of 107.2 ± 1.0–275.4 ± 1.5 µM. Among the synthesized compounds, diethyl derivative 4o and dimethyl derivative 4 h exhibited the highest anti-α-glucosidase activities (IC50 = 107.2 ± 1.0 and 118.0 ± 0.7 µM, respectively). Kinetic analysis of the compound 4o revealed that this compound is a competitive inhibitor for α-glucosidase with Ki value of 113 µM. Furthermore, the docking study on the compounds 4o and 4 h revealed that these compounds interacted with the important residues in the active site of the homology model of α-glucosidase.

Lipases as significant biocatalysts had been widely employed to catalyze various chemical reactions such as ester hydrolysis, ester synthesis, and transesterification. Improving the activity and thermostability of enzymes is desirable for industrial applications. The lipase of Serratia marcescens belonging to family I.3 lipase has a very important pharmaceutical application in production of chiral precursors. In the present study, to achieve improved lipase activity and thermostability, using computational predictions of protein, four mutant lipases of SML (MutG2P, MutG59P, Mut H279K and MutL613WA614P) were constructed by site-directed mutagenesis. The recombinant mutant proteins were over-expressed in E. coli and purified by affinity chromatography on the Ni-NTA system. Circular dichroism spectroscopy, differential scanning calorimetry and kinetic parameters (Km and kcat) were determined. Our results have shown that the secondary structure of all lipases was approximately similar to one another. The MutG2P and MutG59P were more stable than wild type by approximately 2.3 and 2.9 in T1/2, respectively. The catalytic efficiency (kcat/Km) of MutH279K was enhanced by 2-fold as compared with the wild type (p

Ketoconazole is widely used in human and veterinary medicine; however, residual amounts of this antifungal agent have potential adverse effects on ecological health. The present study describes the use of laccase from Trametes versicolor for biotransformation and detoxification of ketoconazole. The substrate was removed at optimum conditions of 45 °C, pH 4.5, incubation time 6 h, ketoconazole concentration 0.3 mg ml−1, 1-hydroxybenzotriazole (HBT) concentration 1 mM, and laccase activity 1 U ml−1. The use of HBT (1 mM), a laccase mediator, enhanced the yield of elimination. A micro-toxicity study with Pseudokirchneriella subcapitata, Candida albicans, Cryptococcus neoformans, and Saccharomyces cerevisiae showed a decrease in the toxicity of laccase-treated ketoconazole and its isolated metabolites. The kinetic parameters Km and Vmax of laccase-catalyzed removal of the substrate were determined as 0.099 μM and 4.43 μmol h−1 mg−1, respectively. Two major bioconverted metabolites were also purified and identified.

Early diagnosis and restoring normal function of dysfunctional endothelium is an attractive strategy for prevention of inflammatory diseases such as atherosclerosis. Inhibition of cell adhesion in the process of atherosclerosis plaque formation, mediated by peptide antagonists of very late antigen-4 (VLA-4) has already been developed and evaluated both in vitro and in vivo. In this study, for the first time, modified ZD7349 (mZD7349) peptide, as an antagonist for VLA-4, was used for targeting fluorescein isothiocyanate-loaded poly (DL-lactic-co-glycolic acid) nanoparticles (FITC-PLGA NPs). Rate of binding and internalization of mZD7349-NPs to activated human umbilical vein endothelial cells (HUVECs) were compared with that of untargeted. Effects of temperature reduction and clathrin-mediated endocytosis inhibitor (0.45M sucrose) were also studied on the binding and internalization of mZD7349-NPs and NPs. Results showed that binding of the conjugated NPs could be significantly blocked by pre-incubating cells with the free peptide, suggesting that the binding of NPs is mediated by attaching the surface peptide to VCAM-1 on HUVECs. Also, conjugated FITC-loaded NPs were shown to be rapidly endocytosized to a greater extent than the unconjugated ones. The binding and internalization of mZD7349-NPs and NPs were slowed down at low temperature and in the presence of sucrose with greater reductions for mZD7349-NPs. To conclude, the peptide-NPs targeting the VCAM-1 is suggested as a theranostic carrier for lesions upregulating VCAM-1.

The aim of this study was to characterize the stability and activity of laccase from Trametes versicolor in the presence of three different surfactants, namely sodium di-2-ethylhexylsulfosuccinate (AOT), Triton X-100 (TX-100), and cetyltrimethylammonium bromide (CTAB). The kinetic parameters (such as K m , k cat , k cat / K m ratio), optimal pH and temperature and the thermostability of the enzyme at different temperatures were determined and compared in the absence and presence of the three surfactants. Results revealed that the catalytic activity of the enzyme was greatly improved in the presence of low concentrations of AOT, whereas the activity declined in the presence of TX-100 and CTAB inactivated it almost completely. Results also depicted that, in general, the presence of the surfactants affected the enzyme optimum pH and temperature. In terms of stability, TX-100-induced stabilization and AOT and CTAB-mediated destabilization of the enzyme were observed. Laccase-mediated bioconversion of indole to 2,2-bis(3′-indolyl)-indoxyl in the presence of TX-100 as the effective stabilizing surfactant and TEMPO as the enzyme mediator was also investigated.

This study describes the enzymatic elimination of imipramine and four other tricyclic antidepressants (TCAs) by laccase-mediated catalysis in aqueous solution. The results showed that TCAs demonstrated dissimilar enzymatic elimination behavior: up to 67% of clomipramine and 82% of imipramine were significantly removed during the first 6 h. The elimination percentages of amitriptyline, doxepin, and nortriptyline were 11%, 6%, and 23%, respectively, after 72 h laccase-based treatment. Due to the rapid and high percentage of removal, imipramine was selected for detailed toxicity evaluation. Optimal levels for the main factors in the enzymatic removal process of imipramine were obtained as pH (4.9), incubation time (5.7 h), imipramine concentration (0.12 μg mL −1 ), and enzyme activity (1.63 U mL −1 ). Laccase-catalyzed transformation of imipramine led to the formation of an unknown metabolite which was subsequently purified and spectroscopically characterized as 3-(2,7-dihydroxy-10,11-dihydro-5 H -dibenzo[ b,f ]azepin-5-yl)-1-hydroxy- N , N -dimethyl-3-oxopropan-1-amine oxide. The toxicity reduction of the bio-product was assessed by MTT cell and Caco-2 cell line.

The aim of the present study was to isolate and identify a terrestrial actinomycete bacterial strain capable to produce selenium nanoparticles (Se NPs) followed by purification of the biogenic Se NPs and evaluation of their photocatalytic degradation compared to selenium dioxide. Among 30 actinomycete bacterial strains obtained from environmental soil samples, one isolate (identified as Streptomyces griseobrunneus strain FSHH12 based on the 16S rDNA gene sequence analysis) was selected and used for production of Se NPs. The biologically synthesized Se NPs was consequently purified by an organic–aqueous partitioning system and characterized using scanning electron microscopy, transmission electron microscopy, energy dispersive X-ray, UV–visible spectroscopy, Fourier transform infrared spectroscopy, and X-ray diffraction spectroscopy. The obtained results of photocatalytic degradation of bromothymol blue using the purified Se NPs (64 μg/mL) revealed 62.3% of dye removal under UV illumination (15 W) a...

In this study, the enzyme streptokinase (thrombolysis agent) and chitosan (Cs) nanoparticles were prepared by self-assembly. Using experimental design, chitosan concentration, solution pH and stirring time were studied as independent variables to identify their effects on size, polydispersity index (PDI) and loading efficiency of nanoparticles. Results showed that pH and concentration have a direct effect on size. Additionally, minimum PDI was observed at lowest values of concentration and highest values of stirring time. pH-5.6 was also necessary to obtain the smallest PDI and highest loading efficiency values. The model predicted that to obtain maximum loading efficiency and minimum size along with low PDI, optimum values are 0.5 mg/mL, 5.18 and 30 min for the Cs concentration, solution pH and stirring time, respectively. The corresponding mean ± SD values for experimentally prepared nanoparticles were 43 ± 10%, 526 ± 121 nm, 0.3 ± 0.2, respectively. MTT and euglobulin clot lysis assays on the optimized nanoparticles showed that chitosan/streptokinase nanoparticles have slightly toxic effect on human fetal lung fibroblast cells (Mrc-5), compared with chitosan and streptokinase alone as a control. Also, thrombolytic activity of encapsulated streptokinase in nanoparticles is decreased slightly in comparison with free streptokinase. However, the preparation keeps a good potency for use as a thrombolytic agent in vivo.

Rising world demand coupled with diminishing supply of fossil fuels and petroleum products have led to look for alternative renewable and clean fuels such as biodiesel. The production of biodiesel can be facilitated with suitable biocatalysts. In the present study, a mesoporous silica of SBA-15 modified with oleic acid and a solvent tolerant lipase from Actinomadura sediminis (SBA-15@oleate@lipase) was designed as the heterogeneous biocatalyst with maximum activity by a protein loading of 32.0 mg per gram of the support. The maximum immobilization efficiency (68%) and yield (80%) were also obtained at 200 µg ml−1 of the protein with reaction time of 60 min. The enzymatic trans-esterification reaction was catalyzed for converting oil of the cyanobacterium Synechococcus elongatus into biodiesel with an 85% ± 3.2 yield under optimized conditions. The designed heterogeneous biocatalyst revealed a high efficiency towards palmitoleic acid (C16:1) in the microalgal oil that is one of the best fatty acids to produce a high-quality biodiesel. This work also highlights the simultaneous combination of purification and immobilization of the bacterial lipase by interfacial activation mechanism, to the synthesis of a solid biocatalyst for production of a cyanobacterium-based biodiesel.

The presence of recalcitrant synthetic dyes in environment is a major concern due to their possible threat on living organisms and aquatic ecosystems. To investigate the potential of combined thermal and enzymatic decolorization, betaine was applied to protect the secondary and tertiary structures as well as the enzymatic activity of laccase under thermal stress. At 60 °C, betaine 1 M significantly enhanced the stability of laccase in addition to keeping its catalytic efficiency (p T m of laccase in the presence of betaine. Once incubated at 60 °C, betaine exhibited superior protein-stabilizing properties than at 25 °C. Furthermore, fluorescence spectroscopy supported this concept that the overall folded structure of laccase became more rigid in the presence of betaine at 60 °C. Betaine-stabilized laccase was used for combined thermal and enzymatic decolorization of some recalcitrant organic dyes. This osmolyte could improve the enzymatic removal of most dyes at 60 °C. A detoxification study with respect to the inhibition of bacterial growth showed a decrease in microtoxicity of the laccase-treated dye solution in the presence of betaine at 60 °C.

Herein, we performed meticulous experimental and computational studies to explore the stability, activity, and dynamics of laccase in the presence of various organic and inorganic solvents. It is well known that laccases are eco-friendly enzymes, which can quickly eliminate recalcitrant chemicals from contaminated media. We determined the Asp96 (COO−)---Arg43 (N-H2), Asp131 (COO−)---Arg197(N-H1), Asp138(COO−)---Arg195 (N-H2), Asp140(COO−)---Arg199(N-H2), Asp214(COO−)---Arg260(N-H2), Asp224(COO−)---Arg423(N-H2), Asp424(COO−)---Arg243(N-H1), Asp424(COO−)---Arg243(N-H2), Glu288(COO−)---Arg176(N-H1) and Glu288(COO−)---Arg176(N-H2) salt bridges as the crucial ones in maintaining the structural integrity of laccase. Furthermore, the fluorescence, circular dichroism (CD) spectroscopies, and molecular dynamics simulation outcomes highlighted that the secondary structure elements and tertiary structure of the enzyme did not change significantly in the presence of both selected organic (ethanol and hexane) and inorganic (1-Butyl-3-methylimidazolium hexafluorophosphate ([BMIM][PF6]) co-solvents. The obtained experimental results demonstrated that the enzyme was more stable in the hexane and aqueous ionic liquid solutions than in the ethanol solution. Additionally, laccase exhibited more activity in the presence of the hexane and aqueous ionic liquid solutions. Probably due to more accessibility of the substrate to the active site of laccase. Interestingly, the activity of laccase in the presence of the co-solvents was in decreasing order of hexane

We herein applied the four step-synthetic route to prepare the pyridazine core attached to the various N-aryl acetamides. By this approach, a new series of pyridazine-based compounds were synthesized, characterized and evaluated for their activities against α-glucosidase enzyme. In-vitro α-glucosidase assay established that twelve compounds are more potent than acarbose. Compound 7a inhibited α-glucosidase with the IC50 value of 70.1 µM. The most potent compounds showed no cytotoxicity against HDF cell line. Molecular docking and kinetic studies were performed to determine the modes of interaction and inhibition, respectively.

Inhibition of α-glucosidase enzyme is of prime importance for the treatment of diabetes mellitus (DM). Apart of many organic scaffolds, pyridine based compounds have previously been reported for wide range of bioactivities. The current study reports a series of pyridine based synthetic analogues for their α-glucosidase inhibitory potential assessed by in vitro, kinetics and in silico studies. For this purpose, 2-amino-4-aryl-6-(phenylthio)pyridine-3,5-dicarbonitriles 1–28 were synthesized and subjected to in vitro screening. Several analogs, including 1–3, 7, 9, 11–14, and 16 showed many folds increased inhibitory potential in comparison to the standard acarbose (IC50 = 750 ± 10 µM). Interestingly, compound 7 (IC50 = 55.6 ± 0.3 µM) exhibited thirteen-folds greater inhibition strength than the standard acarbose. Kinetic studies on most potent molecule 7 revealed a competitive type inhibitory mechanism. In silico studies have been performed to examine the binding mode of ligand (compound 7) with the active site residues of α-glucosidase enzyme.

Bisphenol A (BPA) is an environmental pollutant with adverse effects on different ecosystems. In this study, immobilized laccase enzymes onto inorganic supports were used to remove BPA. Laccase was successfully immobilized on sodium zeolite Y (NaY) and its modified desilicated (DSY) and dealuminated (DAY) forms. NaY-based supports were instrumentally characterized. The immobilized laccase on NaY (laccase@NaY), desilicated (laccase@DSY), and dealuminated (laccase@DAY) forms showed significant improvement on immobilization yield (IY%) and efficiency (IE%). Laccase@DSY and laccase@NaY showed IY% = 73.18 ± 3.33 % and 46.23 ± 1.81 % and IE% = 94.50 ± 1.86 %, and 74.39 ± 1.41 %, respectively, whereas IY% and IE% for laccase@DAY were achieved as 81.12 ± 1.32 % and 98.56 ± 2.93 %, respectively. The supports also increased the enzyme characteristics such as pH-temperature range, catalytic stability, and reusability. Km values were 0.73 ± 0.05, 0.26 ± 0.09, 0.31 ± 0.5, and 1.01 ± 0.03 mM for laccase@NaY, laccase@DAY, laccase@DSY, and the free enzyme, respectively. The enzyme demonstrated higher biodegradation ability of bisphenol A upon immobilization on the supports compared to that of the soluble enzyme. A bio-removal yield of 86.7 % was obtained considering three parameters including amount of laccase@DAY (8 U mg–1), concentration of BPA (0.5 mM), and treatment time (1 h) based on response surface methodology (RSM). Biodegradation metabolites (49 ± 5.8 %) and unconverted BPA (14 ± 5.2 %) were analyzed by gas chromatography-mass spectrometry.

Fucoxanthin is the major abundant xanthophyll in macro- and micro-algae as a component of photosynthetic light-harvesting complexes for photosynthesis and photoprotection. Nowadays, widespread application of fucoxanthin in food industry, pharmaceutical, and medical purposes are increasing. The current issue attracts the attention of researchers for producing of carotenoid from its natural resources, especially algae. Againts macroalgae, microalgae have rapid growth with the same source of food. In addition, they can grow from variety of situations and environmental conditions to produce a specific biochemical product. Microalgae, e.g. Tisochrysis lutea (T. lutea), can be cultivated under controlled conditions, low cost, and higher concentration of fucoxanthin. This review presents some of nutraceutical effects of fucoxanthin for human health and then, in particular, recent biotechnological developments in bioprocessing of this valuable product including, cultivation, harvesting, extraction, and purification, from T. lutea.

Microbial leaching via biocyanidation process enables efficient extraction of precious metals from low-grade ores and increases attention in mineral industries for applying green and environmentally friendly leaching methods. Microbial cyanidation can be applied in cyanidation process mobilizing precious metals from ores and scraps. Biological solubilization processes also recover metals from secondary raw materials such as e-wastes, car catalysts, coins, etc. In comparison with conventional technologies, biomobilization is associated with advantages including simple operation, reduced cost, and less environmental risks. This review was performed to describe a perspective on metal biocyanidation by applying cyanogenic microorganisms. Factors influencing yield of biocyanidation and electrochemical approaches of metal recovery were discussed. This study also addresses future advances of industrial applications of microbial mobilization of some metals as soluble cyanide complex from secondary resources.

In this study, a series of benzimidazole-1,2,3-triazole hybrids 8a-n as new α-glucosidase inhibitors were designed and synthesized. In vitro α-glucosidase inhibition activity results indicated that all the synthesized compounds (IC50 values ranging from 25.2 ± 0.9 to 176.5 ± 6.7 μM) exhibited more inhibitory activity in comparison to standard drug acarbose (IC50 = 750.0 ± 12.5 μM). Enzyme kinetic study on the most potent compound 8c revealed that this compound was a competitive inhibitor into α-glucosidase. Moreover, the docking study was performed in order to evaluation of interaction modes of the synthesized compounds in the active site of α-glucosidase and to explain structure-activity relationships of the most potent compounds and their corresponding analogs.

Background: During last recent years number of anti-tubulin agents were introduced for treatment of diverse kind of cancer. Despite of their potential in treatment of cancer, drug resistance and adverse toxicity such as peripheral neuropathy are some of the negative criteria of anti-tubulin agents. Methods: Twenty seven quinazoline derivatives were synthesized using a multicomponent reaction. The cytotoxicity of compounds 1-27 was tested in SRB assays employing five different human tumor cell lines. Effect of two of active compounds on tubulin polymerization was also checked using a commercially available assay kit. Molecular modelling studies were also performed using autodock tools software. Results: SRB assays showed that compounds 2, 9, 16 and 26, being highly cytotoxic with IC50 values ranging between 2.1 and 14.3µM. The possible mode of action of compounds, 2, 9, 16 and 26, and the taxol binding site of the protein tubulin, an important goal for antimitotic drugs, was also studied by molecular docking, which showed reasonable interactions with tubulin active site, followed by investigation of the effects of compounds 9 and 16 on the polymerization of tubulin. The results showed the tested compounds to be highly active as inducers of tubulin polymerization. Conclusion: Altogether, with respect to obtained results, it is attractive and beneficial to further investigation on quinazoline scaffold as antimitotic agents.

Microalgae are key test organisms to assess the effects of chemicals on aquatic ecosystems. Zinc oxide nanoparticles (ZnO NPs) as a widely used metal oxide is considered a potential threat to these primary producers at the base of the food chain. This study investigates the toxicity of ZnO NPs, bulk ZnO, and Zn2+ to the representative of freshwater microalgae, Raphidocelis subcapitata. To examine the effect of shape and size of nanoparticles, two types of spherical ZnO NPs with different sizes (20 and 40 nm) and two types of rod-shaped ZnO NPs with different lengths (100 and 500 nm) were synthesized. Microalgal cells were exposed to eight concentrations of each ZnO NP type from 0.01 to 0.7 mg/L for 96 h. The results showed that 0.7 mg/L of ZnO NP could completely inhibit algal growth. Size did not interfere with toxicity in spherical ZnO NPs, but the toxicity decreased by increasing the size of rod-shaped ZnO NPs. Spherical ZnO NPs acted more destructive to microalgal cells than nanorod shape. The addition of 0.7 mg/L of ZnO nanorods to samples caused 30% cell death, while 50% cell death was observed by adding the same concentration of nanospherical ZnO. Nano ZnO revealed to be more toxic than bulk ZnO and Zn2+. The Zn2+ released from dissolution of ZnO NPs was one of the sources of toxicity, but the ZnO nanostructures were also an important factor in the toxicity.

Laccase was immobilized using a combinatorial strategy of cross-linking and entrapping in mesoporous silica to prepare entrapped enzyme species including simply adsorbed, entrapped cross-linked enzyme (E-CLE) and entrapped cross-linked enzyme aggregate (E-CLEA) to explore their potential in phenol removal. Parameters including pH, temperature, time and cross-linker concentration were optimized to achieve an immobilized product with highest laccase specific activity. Fourier transform infrared spectroscopy (FT-IR), scanning electron microscopy (SEM) and atomic force microscopy (AFM) were used to characterize the immobilization products. The storage and operational stability analysis were also carried out. Accordingly, E-CLEAs showed improved thermal and pH stabilities and activity retention in hydrophobic and hydrophilic solvents. Moreover, based on the resulted half-lives (t1/2) for free and insoluble laccases, the improved storage stability is reported for E-CLEAs at 1.71 and 20.88 days for them, respectively. In addition, the immobilized biocatalyst exhibited good operational stability and reusability through maintaining up to 79% of its initial activity after 20 cycles of successive operations. In conclusion, E-CLEAs have catalytic potential in efficient phenol removal and advantages of the insolubilized form of laccase as E-CLEAs make it an appealing system in applications such as possible treatment of phenol-contaminated wastewater.

A novel series of acridine linked to thioacetamides 9a–o were synthesized and evaluated for their α-glucosidase inhibitory and cytotoxic activities. All the synthesized compounds exhibited excellent α-glucosidase inhibitory activity in the range of IC50 = 80.0 ± 2.0–383.1 ± 2.0 µM against yeast α-glucosidase, when compared to the standard drug acarbose (IC50 = 750.0 ± 1.5 µM). Among the synthesized compounds, 2-((6-chloro-2-methoxyacridin-9-yl)thio)-N-(p-tolyl) acetamide 9b displayed the highest α-glucosidase inhibitory activity (IC50 = 80.0 ± 2.0 μM). The in vitro cytotoxic assay of compounds 9a–o against MCF-7 cell line revealed that only the compounds 9d, 9c, and 9n exhibited cytotoxic activity. Cytotoxic compounds 9d, 9c, and 9n did not show cytotoxic activity against the normal human cell lines HDF. Kinetic study revealed that the most potent compound 9b is a competitive inhibitor with a Ki of 85 μM. Furthermore, the interaction modes of the most potent compounds 9b and 9f with α-glucosidase were evaluated through the molecular docking studies.

Laccases are versatile multi-copper enzymes belonging to the superfamily of oxidase enzymes, which have been known since the nineteenth century. Recent discoveries have refined investigators' views of the potential of laccase as a magic tool for remarkable biotechnological purposes. A literature review of the capabilities of laccases, their assorted substrates, and their molecular mechanism of action now indicates the emergence of a new direction for laccase application as part of an arsenal in the fight against the contamination of water supplies by a number of frequently prescribed medications. This chapter provides a critical review of the literature and reveals the pivotal role of laccases in the elimination and detoxification of pharmaceutical contaminants in aquatic environments and wastewaters.

Background: Pyrano[3,2-c]quinoline derivatives 6a–n were synthesized via simple two-step reactions and evaluated for their in vitro α-glucosidase inhibitory activity. Methods: Pyrano[3,2-c]quinoline derivatives 6a–n derivatives were prepared from a two-step reaction: cycloaddition reaction between 1-naphthyl amine 1 and malonic acid 2 to obtain benzo[h]quinoline-2(1H)-one 3 and reaction of 3 with aryl aldehydes 4 and Meldrum’s acid 5. The anti- α-glucosidase activity and kinetic study of the synthesized compounds were evaluated using α-glucosidase from Saccharomyces cerevisiae and p-nitrophenyl-a-D-glucopyranoside as substrate. The α-glucosidase inhibitory activity of acarbose was evaluated as positive control. Results: All of the synthesized compounds, except compounds 6i and 6n, showed more inhibitory activity than the standard drug acarbose and were also found to be non-cytotoxic. Among the synthesized compounds, 1-(2-bromophenyl)-1H-benzo[h]pyrano[3,2-c]quinoline-3,12(2H,11H)-dione 6e displayed the highest α-glucosidase inhibitory activity (IC50 = 63.7 ± 0.5 µM). Kinetic study of enzyme inhibition indicated that the most potent compound, 6e, is a non-competitive inhibitor of α-glucosidase with a Ki value of 72 µM. Additionally, based on the Lipinski rule of 5, the synthesized compounds were found to be potential orally active drugs. Conclusion: Our results suggest that the synthesized compounds are promising candidates for treating type 2 diabetes.

The fungal laccase isolated from Paraconiothyrium variabile was applied to optimize the enzymatic decolorization and detoxification of the azo dye reactive orange 7 using response surface methodology. Initial screening using fractional factorial design was carried out to select important independent variables that significantly affect the yield of decolorization including enzyme activity, pH, and incubation time. Optimum condition for maximal dye decolorization obtained by central composite design and surface plots were laccase activity 1.25 U/mL, pH 6.0, and incubation time 12.5 min. In addition, the kinetic and energetic parameters for enzymatic decolorization of reactive orange 7 were studied and the calculated values for Km, Vmax, Ea, ΔH, and ΔS were 1.14 mM, 283.28 mM/min.mg, 40 kJ/mol, 89 kJ/mol, and 285 J/mol.K, respectively. Decolorization is endothermic and spontaneous at temperatures higher than 37.8 °C. Microtoxicity evaluation demonstrated a decrease in toxicity of the laccase-treated dye in comparison with the parent dye.

Herein we reported the structure and several properties of a new biosurfactants produced by Corynebacterium xerosis strain NS5. This strain was capable of producing a novel lipopeptide biosurfactant that we have named coryxin. The biosurfactant structure was characterized by using Fourier transform infrared spectroscopy (FTIR), Nuclear magnetic resonance spectroscopy (NMR), and Liquid chromatography-mass spectrometry (LC-MS). It contained a hydrophobic moiety of 3-hydroxydecanoic acid and a peptide part predicted as a sequence of seven amino acids including Asn-Arg-Asn-Gln-Pro-Asn-Ser. Coryxin lowered the surface tension of water to 31.4 mN/m, with a critical micelle concentration of 25mg/l. It was a strong emulsifier with an emulsification index of 61% against n-hexane. Coryxin showed antibacterial activity against test organisms belonging to Gram-positive and Gram-negative bacteria and disrupted preformed biofilms of Staphylococcus aureus (82.5%), Streptococcus mutans (80%), Escherichia coli (66%) and Pseudomonas aeruginosa (30%). In conclusion, microbial surfactant from C. xerosis exhibited inhibitory and disruptive activities against biofilm formation that could be of use in biofilm-related menace.

Laccases are phenol oxidases belonging to the superfamily of multicopper oxidases and are found in bacteria, fungi, lichens, higher plants, and insects. Over the past few decades, laccases and laccase mediator systems (LMS) have found uses in a wide range of technological applications such as textile dye decolorization, industrial wastewater detoxification, pulp bleaching, chemical synthesis, and development of miniaturized biosensors. This has encouraged numerous studies to find and purify laccases with exploitable characteristics. The main aim of the present review is to summarize the rich literature data gained in recent years from the studies on laccases, focusing on the organisms that produce them, the methods used for screening, laccase activity assays, purification strategies, and the application of laccases as eco-friendly biocatalysts.

In this study, polyethylenimine coated Fe3O4 magnetic nanoparticles (Fe@PEI) were prepared and used for three metal ions (Co2+, Cu2+ and Pd2+) chelation. The metal chelated magnetic nanoparticles (Fe@PEI-M) were characterized by using different spectroscopic and analytical techniques. The metal contents were analyzed by inductively coupled plasma atomic emission spectroscopy (ICP) and energy-dispersive X-ray spectroscopy (EDX). Thermomyces lanuginosa lipase (TLL) was then immobilized onto the modified magnetic supports by physical adsorption. Fe@PEI-Co and Fe@PEI-Cu showed better activity at extreme temperature and pH values than of the free enzyme. After 10 cycles of successful biocatalytic activity performed by immobilized lipase on Fe@PEI-Co, more than 60% of initial activity was reserved. Furthermore, the immobilized lipase onto Fe@PEI-Co retained about 80% of its initial activity after 14 days of storage. The immobilized lipase on the selected nanocomposite was then used for synthesis of ethyl valerate. After 24 h incubation time, the extent of esterification was found to be 70 and 60% in n-hexane and DMSO media, respectively.

The lipase of Serratia marcescens (SML), containing 614 amino acid residues and belonging to the lipase family I.3, has an important pharmaceutical application in production of chiral precursors. Similar to other members of this family, the SML consists of the N-catalytic domain (α/β) that contains the active-site residues and the C-terminal domain that includes the two parallel β-roll domains, the first and second β-roll. The repetitive sequences, a nine-residue sequence motif (GGXGXDXUX), in SML are somewhat degenerated as well as not consecutive. The parallel β-roll domains are separated from each other by a 72-residue spacer. The importance of these repetitive sequences has not been fully understood yet. In the present investigation, as an approach, a C-terminally truncated (∼13 kD) SML was generated using a polymerase chain reaction (PCR)-based site-directed mutagenesis method (designated SML-Δ128). Both wild-type and truncated forms of SML were constructed, overexpressed in Escherichia coli without the Lip system and purified by affinity chromatography on the Ni-NTA system. The kinetic parameters and circular dichroism (CD) spectra were determined and compared. The SML-Δ128 showed an approximately 3.7-fold increase in the turnover rate ( k cat ), relative to that of the full-length enzyme. In conclusion, this report demonstrates that the SML could tolerate extensive modification in the C-terminal extreme of the protein, as deletion of the C-terminal region (∼13 kDa), which consists of several tandem repeats of glycine-rich and 49 residues including the signal peptide, significantly increases the catalytic efficiency of the enzyme.

Hypercholesterolemia is an important risk factor contributing to atherosclerosis and coronary heart disease. Lactic acid bacteria have attracted much attention regarding their promising effect on serum cholesterol levels. Tellurium (Te) is a rare element that has also gained considerable interest for its biological effects. There have been some recent in vivo reports on the reduction effect of Te on cholesterol content. In this study, Lactobacillus plantarum PTCC 1058 was employed for the intracellular biosynthesis of Te NPs. The UV-visible spectrum of purified NPs showed a peak at 214 nm related to the surface plasmon resonance of the Te NPs. Transmission electron microscopy showed that spherical nanoparticles without aggregation had the average size of 45.7 nm as determined by the laser scattering method. The energy dispersive X-ray pattern confirmed the presence of Te atoms without any impurities. A significant reduction was observed in group which received L. plantarum with or without Te NPs during propylthiouracil and cholesterol diet in compare with the control group which received just propylthiouracil and cholesterol. The levels of triglycerides also remarkably decrease (p

The performance of hollow fiber membrane photobioreactors (HFMPB) for the growth of Synechococcus elongatus at various CO2 concentrations (0.04% (ambient air), 10% and 15%) and medium re-circulation flow rates (34.4, 60 and 86.6 mL/min) was studied. Cultivation was carried out at both batch and semi-continuous modes in HFMPBs containing neat and hydrophilized in-house fabricated poly propylene (PP) membranes at a fixed light intensity of 3000 lux and temperature of 27oC. Cyanobacterium showed better growth at 10% CO2 at an initial pH = 8.2 using BG11 medium in both cultivation modes and modules. Maximum biomass concentration, CO2 biofixation and specific growth rates equal with 2.1 g L–1, 2.08 g L–1d–1 and 1.76 d–1 were obtained for non-wetted membranes, respectively. Comparing the performance of both modules showed that the impact of cultivation mode on the CO2 biofixation rate and CO2 removal is more influential than the impact of mass transfer resistance in membrane contactors.

In this paper, the enzymatic detoxification of aflatoxin B1 (AFB1) by laccase was studied, and the prooxidant properties and mutagenicity of the detoxification products were compared with those of AFB1. The optimal enzymatic reaction occurred in 0.1M of citrate buffer containing 20% DMSO at 35 °C, a pH of 4.5, and a laccase activity of 30 U mL(-1). After 2 d, sixty-seven percent of the toxic substrate was removed. The prooxidative properties of the detoxified products (27% versus 86%) and the mutagenicity were significantly decreased in comparison with the parent toxin. Unlike AFB1, which promoted metabolism-dependent genetic mutations by base-pair substitution, the detoxified products did not induce genotoxicity. Comparison of the Km values for AFB1 and riboflavin, a valuable food nutrient, indicated that laccase showed greater affinity for the toxin than for riboflavin.

Response surface methodology (RSM) was applied to optimize the removal of flumequine (FLU) from aqueous solution by laccase from Trametes versicolor. Box–Behnken design (BBD) with four variables namely pH, temperature, FLU initial concentration, and 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) concentration was used to optimize these factors. The results showed that the predicted values for FLU removal were close to the experimental values, and the R2 (0.9967) indicated that the regression was able to give a good prediction of response for the FLU removal process in the studied range. Optimization of the factors levels was carried out in two approaches. At first, all factors were set in the studied range. The selected optimal conditions for the maximum removal of FLU (98.27%) were predicted as: temperature of 39.64°C, pH of 4.06, FLU initial concentration of 90.74 mg L−1, and ABTS concentration of 1.35 mM. Then, the optimization was carried out by minimizing the amount of ABTS, maxim...

Background: Tumor associated antigens can be viably used to enhance host immune response. Objectives: The immunomodulatory effect of biogenic selenium nanoparticles (SeNPs) was compared between treated and untreated mice with crude antigens of 4T1 cells. Materials and Methods: Female inbred BALB/c mice (60) were injected by cancinogenic 4T1 cells causing breast cancer. After 10 days, all tumor bearing mice were divided into 4 groups. Group 1 was daily provided oral PBS and injected by the same buffer after tumor induction and was considered as control. Group 2 received only 100 mg/day SeNPs as an oral supplement for 30 days. Group 3 was only injected with 4T1 cells crude antigens with nil supplementation of SeNPs. Group 4 animals were supplemented 100 mg/day SeNPs for 30 days and simultaneously injected with crude antigens of 4T1 cells. All antigens or PBS injections were introduced at 7, 14 and 28 days following tumor induction. Oral PBS and SeNPs supplementation initiated from the first day of tumor induction and continued up to 30 days. During tumor growth, animal weights and survival rates were monitored and at the end of the study the concentrations of different cytokines and DTH responses were measured. Results: Data clearly showed that the levels of cellular immunomodulatory components (granzyme B, IL-12, IFN-g, and IL-2) significantly increased (P < 0.05) in mice treated with both SeNPs and crude antigens of 4T1 cells in comparison to the other groups. In contrast, the levels of TGF-b in these mice decreased. Conclusions: Although SeNPs showed a noticeable boosting effect for the immune response in mice bearing tumor exposed to crude antigens of 4T1 cells, further complementary studies seem to be inevitable.

In this research, the kinetics and equilibrium of nickel(II) biosorption were studied in aqueous solutions using batch technique. The biosorption was carried on Ca-alginate beads, on nonliving mycelium of Aspergillus awamori immobilized on Ca-alginate, and on free fungal biomass. The biosorbents were characterized by FTIR and SEM analyses. The experimental data were analyzed in terms of pseudo-first-order, pseudo-second-order, and intraparticle diffusion kinetic models. It was observed that the biosorption process of Ni(II) ions followed well pseudo-second-order model on all biosorbents. The experimental results showed that biosorption equilibrium on blank Ca-alginate, free biomass, and immobilized fungal biomass fit better to the Langmuir model when compared with the Freundlich model in concentration range studied (25–75 mg L−1). The results showed that the maximum monolayer biosorption capacity of the immobilized fungal biosorbent was 8.34 mg g−1 when compared with the blank Ca-alginate and free biomass with 4.63 and 7.13 mg g−1, respectively. © 2015 American Institute of Chemical Engineers Environ Prog, 34: 1356–1364, 2015

Biocompatible multi-layer iron oxide magnetic nanoparticles (MNPs) for drug delivery applications with increased loading capacity, sustained sensitive release profile, and high inherent magnetic properties as well as improved cellular uptake were prepared. In this approach, Fe3O4 MNPs were obtained by a co-precipitation method and functionalized using hydroxyapatite (HAP) and/or polyethyleneimine (PEI). They were then modified with β-cyclodextrin (CD) to increase their loading capacity. These MNPs allowed suitable encapsulation of hydrophobic curcumin (CUR) in the CD shell and CUR adsorption into the polymeric layers. The dissolution profile of CUR showed pH sensitive release of CUR. The protein corona pattern of the MNPs by electrophoresis showed lower protein adsorption for CD modified MNPs than for other MNPs. No significant toxicity was observed for the target MNPs, whereas the CUR loaded MNPs inhibited MCF-7 breast cancer cells more efficiently than free CUR. Moreover, the negligible hemolytic activity of the target MNPs showed their excellent haemocompatibility for cancer treatment. The preferential uptake of the drug by MCF-7 cells was observed for CUR loaded MNPs in comparison with free CUR using flow cytometric analysis. As a result, the designed and prepared MNPs can be considered to be a promising CUR delivery platform.