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32 results on '"Arnusch, Christopher J."'

11. Bacterial surface attachment and fouling assay on polymer and carbon surfaces using Rheinheimera sp. identified using bacteria community analysis of brackish water

Author

Manderfeld, Emily, Thamaraiselvan, Chidambaram, Kleinberg, Maurício Nunes, Jusufagic, Lejla, Arnusch, Christopher J., and Rosenhahn, Axel

Subjects
Aquatic Science, Applied Microbiology and Biotechnology, Water Science and Technology
Abstract

Biofouling on surfaces in contact with sea- or brackish water can severely impact the function of devices like reverse osmosis modules. Single species laboratory assays are frequently used to test new low fouling materials. The choice of bacterial strain is guided by the natural population present in the application of interest and decides on the predictive power of the results. In this work, the analysis of the bacterial community present in brackish water from Mashabei Sadeh, Israel was performed and Rheinheimera sp. was detected as a prominent microorganism. A Rheinheimera strain was selected to establish a short-term accumulation assay to probe initial bacterial attachment as well as biofilm growth to determine the biofilm-inhibiting properties of coatings. Both assays were applied to model coatings, and technically relevant polymers including laser-induced graphene. This strategy might be applied to other water sources to better predict the fouling propensity of new coatings.

Published
2022
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13. Virus Inactivation in Water Using Laser-Induced Graphene Filters

Author

Barbhuiya, Najmul Haque, primary, Singh, Swatantra P., additional, Makovitzki, Arik, additional, Narkhede, Pradnya, additional, Oren, Ziv, additional, Adar, Yaakov, additional, Lupu, Edith, additional, Cherry, Lilach, additional, Monash, Arik, additional, and Arnusch, Christopher J., additional

Published
2021
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18. Attachment of antimicrobial peptides to reverse osmosis membranes by Cu(i)-catalyzed 1,3-dipolar alkyne-azide cycloaddition

Author

Bodner, Elias J., Kandiyote, Nitzan Shtreimer, Lutskiy, Marina Yamit, Albada, Bauke, Metzler-Nolte, Nils, Uhl, Wolfgang, Kasher, Roni, Arnusch, Christopher J., Bodner, Elias J., Kandiyote, Nitzan Shtreimer, Lutskiy, Marina Yamit, Albada, Bauke, Metzler-Nolte, Nils, Uhl, Wolfgang, Kasher, Roni, and Arnusch, Christopher J.

Abstract

Biofilms are detrimental to many industrial systems that include reverse osmosis (RO) membranes. Accordingly, the development of surfaces with inherently bactericidal properties has attracted much research attention. Antimicrobial peptides (AMPs) have been shown to be potent antimicrobial and anti-biofilm agents. In the current study, we developed an efficient synthetic procedure for AMP immobilization on RO membranes which is based on the copper(i) mediated Huisgen 1,3-dipolar cycloaddition reaction ("click chemistry"). Optimization of the reaction temperature, time, peptide and catalyst concentration resulted in efficient coupling of peptides to the membrane surface. The reaction conditions did not affect membrane salt rejection, and resulted in only a slight reduction (14%) in pure water flux at the highest temperature tested (80 °C). Short AMPs that consisted of Arg-Trp repeats were attached onto a virgin RO membrane surface, and an RO membrane surface coated with a copolymer of methacrylic acid and poly(ethylene glycol)methacrylate. In a bacterial contact killing assay, the resulting peptide-modified membrane surfaces showed increased antimicrobial activity especially on the virgin membrane as compared to unmodified membranes. This study provides a basis for further research into the attachment of a wide variety of antimicrobials or other entities to surfaces.

Published
2016

21. Interference of the galactose-dependent binding of lectins by novel pentapeptide ligands

Author

Arnusch, Christopher J., André, Sabine, Valentini, Paola, Lensch, Martin, Russwurm, Roland, Siebert, Hans-Christian, Fischer, Marcel J. E., Gabius, Hans-Joachim, Pieters, Roland J., Dep Farmaceutische wetenschappen, Afd Chemical Biology and Drug Discovery, Dep Farmaceutische wetenschappen, and Afd Chemical Biology and Drug Discovery

Subjects
Stereochemistry, Clinical Biochemistry, Molecular Sequence Data, galactose, Pharmaceutical Science, pentapeptide, protein binding, Ligands, ligand, Biochemistry, Pentapeptide repeat, protein modification, chemistry.chemical_compound, Lectins, Drug Discovery, Amino Acid Sequence, Peptide library, Molecular Biology, Peptide sequence, Galectin, galectin, biology, Dose-Response Relationship, Drug, Binding protein, Organic Chemistry, Rational design, article, Lectin, Galactose, library, amino acid sequence, nuclear magnetic resonance, chemistry, carbohydrate, protein analysis, biology.protein, Molecular Medicine, lectin, Oligopeptides, Protein Binding
Abstract

A library of pentapeptides containing the sequence -Y-X-Y- based on rational design was screened with six different lectins. Sequences were identified that modulate galectin binding to its natural carbohydrate ligand. SPR showed inhibition values 2-3 times stronger than galactose and NMR studies suggested real carbohydrate mimicry. © 2004 Elsevier Ltd. All rights reserved.

Published
2004

22. Synthesis of multivalent Streptococcus suis adhesion inhibitors by enzymatic cleavage of polygalacturonic acid and 'click' conjugation

Author

Dep Farmaceutische wetenschappen, Sub Medicinal Chemistry & Chemical biol., Dep Scheikunde, Medicinal Chemistry, Afd Chemical Biology and Drug Discovery, Branderhorst, Hilbert M., Kooij, Raymond, Salminen, Annika, Jongeneel, Lieneke H., Arnusch, Christopher J., Liskamp, Rob M. J., Finne, Jukka, Pieters, Roland J., Dep Farmaceutische wetenschappen, Sub Medicinal Chemistry & Chemical biol., Dep Scheikunde, Medicinal Chemistry, Afd Chemical Biology and Drug Discovery, Branderhorst, Hilbert M., Kooij, Raymond, Salminen, Annika, Jongeneel, Lieneke H., Arnusch, Christopher J., Liskamp, Rob M. J., Finne, Jukka, and Pieters, Roland J.

Published
2008

23. Enhanced membrane pore formation by multimeric/oligomeric antimicrobial peptides

Author

Dep Farmaceutische wetenschappen, Dep Scheikunde, Aandachtsgebieden, Medicinal Chemistry, Chemical Biology 1, Afd Chemical Biology and Drug Discovery, Arnusch, Christopher J., Branderhorst, Hilbert, De Kruijff, Ben, Liskamp, Rob M. J., Breukink, Eefjan, Pieters, Roland J., Dep Farmaceutische wetenschappen, Dep Scheikunde, Aandachtsgebieden, Medicinal Chemistry, Chemical Biology 1, Afd Chemical Biology and Drug Discovery, Arnusch, Christopher J., Branderhorst, Hilbert, De Kruijff, Ben, Liskamp, Rob M. J., Breukink, Eefjan, and Pieters, Roland J.

Published
2007

24. Identification of peptide ligands for malignancy- and growth-regulating galectins using random phage-display and designed combinatorial peptide libraries

Author

Dep Farmaceutische wetenschappen, Afd Chemical Biology and Drug Discovery, André, Sabine, Arnusch, Christopher J., Kuwabara, Ichiro, Russwurm, Roland, Kaltner, Herbert, Gabius, Hans-Joachim, Pieters, Roland J., Dep Farmaceutische wetenschappen, Afd Chemical Biology and Drug Discovery, André, Sabine, Arnusch, Christopher J., Kuwabara, Ichiro, Russwurm, Roland, Kaltner, Herbert, Gabius, Hans-Joachim, and Pieters, Roland J.

Published
2005

28. Interference of the galactose-dependent binding of lectins by novel pentapeptide ligands

Author

Dep Farmaceutische wetenschappen, Afd Chemical Biology and Drug Discovery, Arnusch, Christopher J., André, Sabine, Valentini, Paola, Lensch, Martin, Russwurm, Roland, Siebert, Hans-Christian, Fischer, Marcel J. E., Gabius, Hans-Joachim, Pieters, Roland J., Dep Farmaceutische wetenschappen, Afd Chemical Biology and Drug Discovery, Arnusch, Christopher J., André, Sabine, Valentini, Paola, Lensch, Martin, Russwurm, Roland, Siebert, Hans-Christian, Fischer, Marcel J. E., Gabius, Hans-Joachim, and Pieters, Roland J.

Published
2004

31. Synthesis of multivalent Streptococcus suis adhesion inhibitors by enzymatic cleavage of polygalacturonic acid and ‘click’ conjugation

Author

Branderhorst, Hilbert M., Kooij, Raymond, Salminen, Annika, Jongeneel, Lieneke H., Arnusch, Christopher J., Liskamp, Rob M. J., Finne, Jukka, Pieters, Roland J., Dep Farmaceutische wetenschappen, Sub Medicinal Chemistry & Chemical biol., Dep Scheikunde, Medicinal Chemistry, Afd Chemical Biology and Drug Discovery, Dep Farmaceutische wetenschappen, Sub Medicinal Chemistry & Chemical biol., Dep Scheikunde, Medicinal Chemistry, and Afd Chemical Biology and Drug Discovery

Subjects
Dendrimers, Streptococcus suis, synthesis, Stereochemistry, Chemical structure, Molecular Sequence Data, Disaccharide, polygalacturonase, Disaccharides, dendrimer, chemistry, Cleavage (embryo), Biochemistry, chemistry.chemical_compound, 4 O alpha D galactopyranosyl D galactose, dose response, Dendrimer, carbohydrate analysis, pathogenicity, Trisaccharide, Physical and Theoretical Chemistry, pectin, chemistry.chemical_classification, Hemagglutination assay, Dose-Response Relationship, Drug, Molecular Structure, biology, drug effect, Organic Chemistry, article, 4-O-alpha-D-galactopyranosyl-D-galactose, cell adhesion, Hemagglutination Inhibition Tests, biology.organism_classification, unclassified drug, Enzyme, Carbohydrate Sequence, sensitivity and specificity, molecular genetics, chemical structure, Pectins, polygalacturonic acid, hemagglutination inhibition test, disaccharide
Abstract

A galabiose disaccharide building block was synthesized by an efficient pectinase cleavage of polygalacturonic acid and subsequent chemical functional group transformations. Besides the disaccharide, the corresponding trisaccharide was also obtained and modified. The compounds were subsequently conjugated to dendrimers with up to eight end groups using 'click' chemistry. The compounds were evaluated as inhibitors of adhesion of the pathogen Streptococcus suis in a hemagglutination assay and strong inhibition was observed for the tetra- and octavalent galabiose compound with MIC values in the low nanomolar range. The corresponding octavalent trisaccharide was a ca. 20-fold weaker inhibitor.

Published
2008
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32. Ultrashort Peptide Bioconjugates Are Exclusively Antifungal Agents and Synergize with Cyclodextrin and Amphotericin B

Author

Arnusch, Christopher J., Ulm, Hannah, Josten, Michaele, Shadkchan, Yana, Osherov, Nir, Sahl, Hans-Georg, and Shai, Yechiel

Abstract

ABSTRACTMany natural broad-spectrum cationic antimicrobial peptides (AMPs) possess a general mode of action that is dependent on lipophilicity and charge. Modulating the lipophilicity of AMPs by the addition of a fatty acid has been an effective strategy to increase the lytic activity and can further broaden the spectrum of AMPs. However, lipophilic modifications that narrow the spectrum of activity and exclusively direct peptides to fungi are less common. Here, we show that short peptide sequences can be targeted to fungi with structured lipophilic biomolecules, such as vitamin E and cholesterol. The conjugates were active against Aspergillus fumigatus, Cryptococcus neoformans, and Candida albicansbut not against bacteria and were observed to cause membrane perturbation by transmission electron microscopy and in membrane permeability studies. However, for C. albicans, selected compounds were effective without the perturbation of the cell membrane, and synergism was seen with a vitamin E conjugate and amphotericin B. Moreover, in combination with β-cyclodextrin, antibacterial activity emerged in selected compounds. Biocompatibility for selected active compounds was tested in vitroand in vivousing toxicity assays on erythrocytes, macrophages, and mice. In vitrocytotoxicity experiments led to selective toxicity ratios (50% lethal concentration/MIC) of up to 64 for highly active antifungal compounds, and no in vivomurine toxicity was seen. Taken together, these results highlight the importance of the conjugated lipophilic structure and suggest that the modulation of other biologically relevant peptides with hydrophobic moieties, such as cholesterol and vitamin E, generate compounds with unique bioactivity.

Published
2011
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