5 results on '"Pashandi, Zaiddodine"'
Search Results
2. Curcumin-loaded nanofibers for targeting endometriosis in the peritoneum of a mouse model.
- Author
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Boroumand, Safieh, Hosseini, Sara, Pashandi, Zaiddodine, Faridi-Majidi, Reza, and Salehi, Mohammad
- Subjects
PELVIC pain ,PELVIS ,NANOFIBERS ,PERITONEUM ,DRUG delivery systems ,ETHYLENE glycol - Abstract
Endometriosis is a common, chronic gynecological disorder associated with ongoing pelvic pain, infertility, and adhesions in reproductive age women. Current therapeutic strategies are not effective and the recurrent nature of endometriosis makes it difficult to treat. In this study, we have designed a drug delivery system to control sustained and prolonged release of curcumin in the peritoneum and pelvic cavity of a mouse model of endometriosis. Poly ε-Caprolactone (PCL) and poly ethylene glycol (PEG) polymers were used to synthesize curcumin loaded nanofibers. After scanning electron microscopy (SEM) observation of the nanofiber's morphology, we evaluated the drug release profile and in vitro degradation rate of the curcumin-loaded nanofibers. Next, we tested these nanofibers in vivo in the peritoneum of an endometriosis mouse model to determine their anti-endometriosis effects. Histological evaluations were also performed. Curcumin loaded nanofibers were successfully synthesized in the 8 and 10 wt% polymers. The release test of the curcumin-loaded nanofibers showed that approximately 23% of the loaded curcumin was released during 30 min, 35% at 24 h, and 50% at 30 days. Endometriosis was successfully induced in Balb/c mice, as noted by the observed characteristics of endometriosis in all of the mice and confirmation of endometriosis by hematoxylin and eosin (H&E) staining. In vivo experiments showed the ability of these implanted curcumin loaded nanofibers to mitigate endometriosis. We observed a considerable reduction in the endometrial glands and stroma, along with significant reduction in infiltration of inflammatory cells. Implantable curcumin loaded nanofibers successfully mitigated intraperitoneal endometriosis. [ABSTRACT FROM AUTHOR]
- Published
- 2020
- Full Text
- View/download PDF
3. QM/MM simulations provide insight into the mechanism of bioluminescence triggering in ctenophore photoproteins.
- Author
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Molakarimi, Maryam, Mohseni, Ammar, Taghdir, Majid, Pashandi, Zaiddodine, Gorman, Michael A., Parker, Michael W., Naderi-Manesh, Hossein, and Sajedi, Reza H.
- Subjects
BIOLUMINESCENCE ,SIMULATION methods & models ,CTENOPHORA ,CHROMOPHORES ,MOLECULAR dynamics ,POLAR solvents - Abstract
Photoproteins are responsible for light emission in a variety of marine ctenophores and coelenterates. The mechanism of light emission in both families occurs via the same reaction. However, the arrangement of amino acid residues surrounding the chromophore, and the catalytic mechanism of light emission is unknown for the ctenophore photoproteins. In this study, we used quantum mechanics/molecular mechanics (QM/MM) and site-directed mutagenesis studies to investigate the details of the catalytic mechanism in berovin, a member of the ctenophore family. In the absence of a crystal structure of the berovin-substrate complex, molecular docking was used to determine the binding mode of the protonated (2-hydroperoxy) and deprotonated (2-peroxy anion) forms of the substrate to berovin. A total of 13 mutants predicted to surround the binding site were targeted by site-directed mutagenesis which revealed their relative importance in substrate binding and catalysis. Molecular dynamics simulations and MM-PBSA (Molecular Mechanics Poisson-Boltzmann/surface area) calculations showed that electrostatic and polar solvation energy are +115.65 and -100.42 kcal/mol in the deprotonated form, respectively. QM/MM calculations and pKa analysis revealed the deprotonated form of substrate is unstable due to the generation of a dioxetane intermediate caused by nucleophilic attack of the substrate peroxy anion at its C
3 position. This work also revealed that a hydrogen bonding network formed by a D158- R41-Y204 triad could be responsible for shuttling the proton from the 2- hydroperoxy group of the substrate to bulk solvent. [ABSTRACT FROM AUTHOR]- Published
- 2017
- Full Text
- View/download PDF
4. Comparative Proteomic Study Reveals the Molecular Aspects of Delayed Ocular Symptoms Induced by Sulfur Mustard.
- Author
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Pashandi, Zaiddodine, Saraygord-Afshari, Neda, Naderi-Manesh, Hossein, and Naderi, Mostafa
- Abstract
Objective. Sulfur mustard (SM) is a highly reactive alkylating agent which produces ocular, respiratory, and skin damages. Eyes are the most sensitive organ to SM due to high intrinsic metabolic and rapid turnover rate of corneal epithelium and aqueous-mucous interfaces of the cornea and conjunctiva. Here we investigate underlying molecular mechanism of SM exposure delayed effects which is still a controversial issue after about 30 years. Materials and Methods. Following ethical approval, we have analyzed serum proteome of ten severe SM exposed male patients with delayed eye symptoms with two-dimensional electrophoresis followed by matrix-assisted laser desorption/ionization time-of-flight/time-of-flight mass spectrometry. The western blotting was used to confirm the proteins that have been identified. Results. We have identified thirteen proteins including albumin, haptoglobin, and keratin isoforms as well as immunoglobulin kappa chain which showed upregulation while transferrin and alpha 1 antitrypsin revealed downregulation in these patients in comparison with healthy control group. Conclusions. Our results elevated participation of free iron circulatory imbalance and local matrix-metalloproteinase activity in development of delayed ocular symptoms induced by SM. It demonstrates that SM induced systemic toxicity leads to some serum protein changes that continually and gradually exacerbate the ocular surface injuries. [ABSTRACT FROM AUTHOR]
- Published
- 2015
- Full Text
- View/download PDF
5. PUTRACER: A NOVEL METHOD FOR IDENTIFICATION OF CONTINUOUS-DOMAINS IN MULTI-DOMAIN PROTEINS.
- Author
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ARAB, SEYED SHAHRIAR, GHARAMALEKI, MOHAMMADBAGHER PARSA, PASHANDI, ZAIDDODINE, and MOBASSERI, REZVAN
- Subjects
BIOINFORMATICS ,PROTEIN structure ,PHARMACOLOGY ,HYDROGEN bonding ,THREE-dimensional imaging in biology ,PROTEIN drugs ,MEDICINE - Abstract
Computer assisted assignment of protein domains is considered as an important issue in structural bioinformatics. The exponential increase in the number of known three dimensional protein structures and the significant role of proteins in biology, medicine and pharmacology illustrate the necessity of a reliable method to automatically detect structural domains as protein units. For this aim, we have developed a program based on the accessible surface area (ASA) and the hydrogen bonds energy in protein backbone (HBE). PUTracer (Protein Unit Tracer) is built on the features of a fast top-down approach to cut a chain into its domains (contiguous domains) with minimal change in ASA as well as HBE. Performance of the program was assessed by a comprehensive benchmark dataset of 124 protein chains, which is based on agreement among experts (e.g. CATH, SCOP) and was expanded to include structures with different types of domain combinations. Equal number of domains and at least 90% agreement in critical boundary accuracy were considered as correct assignment conditions. PUTracer assigned domains correctly in 81.45% of protein chains. Although low critical boundary accuracy in 18.55% of protein chains leads to the incorrect assignments, adjusting the scales causes to improve the performance up to 89.5%. We discuss here the success or failure of adjusting the scales with provided evidences. Availability: PUTracer is available at [ABSTRACT FROM AUTHOR]
- Published
- 2013
- Full Text
- View/download PDF
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