Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Bee-Ha Gan"'
Autor:
Thissa N. Siriwardena, Bee-Ha Gan, Thilo Köhler, Christian van Delden, Sacha Javor, Jean-Louis Reymond
Publikováno v:
ACS Central Science, Vol 7, Iss 1, Pp 126-134 (2021)
Externí odkaz:
https://doaj.org/article/1e0e6c66d0f746cf81978a1346cbb050
Publikováno v:
Molecules, Vol 25, Iss 23, p 5643 (2020)
There is an urgent need to develop new antibiotics against multidrug-resistant bacteria. Many antimicrobial peptides (AMPs) are active against such bacteria and often act by destabilizing membranes, a mechanism that can also be used to permeabilize b
Externí odkaz:
https://doaj.org/article/a52c2c8a3ee845d082f9ca687d4950b9
Autor:
Jean-Louis Reymond, Sacha Javor, Christian van Delden, Thilo Köhler, Bee-Ha Gan, Thissa N. Siriwardena
Publikováno v:
ACS Central Science
Siriwardena, Thissa N.; Gan, Bee-Ha; Köhler, Thilo; van Delden, Christian; Javor, Sacha; Reymond, Jean-Louis (2021). Stereorandomization as a Method to Probe Peptide Bioactivity. ACS central science, 7(1), pp. 126-134. ACS Publications 10.1021/acscentsci.0c01135
ACS Central Science, Vol 7, Iss 1, Pp 126-134 (2021)
Siriwardena, Thissa N.; Gan, Bee-Ha; Köhler, Thilo; van Delden, Christian; Javor, Sacha; Reymond, Jean-Louis (2021). Stereorandomization as a Method to Probe Peptide Bioactivity. ACS central science, 7(1), pp. 126-134. ACS Publications 10.1021/acscentsci.0c01135
ACS Central Science, Vol 7, Iss 1, Pp 126-134 (2021)
Solid-phase peptide synthesis (SPPS) is usually performed with optically pure building blocks to prepare peptides as single enantiomers. Herein we report that SPPS using racemic amino acids provides stereorandomized (sr) peptides, containing up to bi
Autor:
Viorica Patrulea, Bee-Ha Gan, Karl Perron, Xingguang Cai, Philippe Abdel-Sayed, Emmanuelle Sublet, Verena Ducret, Natalia Porroche Nerhot, Lee Ann Applegate, Gerrit Borchard, Jean-Louis Reymond, Olivier Jordan
Publikováno v:
Patrulea, Viorica; Gan, Bee-Ha; Perron, Karl; Cai, Xingguang; Abdel-Sayed, Philippe; Sublet, Emmanuelle; Ducret, Verena; Nerhot, Natalia Porroche; Applegate, Lee Ann; Borchard, Gerrit; Reymond, Jean-Louis; Jordan, Olivier (15 March 2022). Synergistic effects of antimicrobial peptide dendrimer-chitosan polymer conjugates against Pseudomonas aeruginosa. Carbohydrate polymers, 280, p. 119025. Elsevier 10.1016/j.carbpol.2021.119025
We report herein a new chemical platform for coupling chitosan derivatives to antimicrobial peptide dendrimers (AMPDs) with different degrees of ramification and molecular weights via thiol-maleimide reactions. Previous studies showed that simple inc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d318e878afe5fd9666f6a38477be332
Autor:
Ana S. Ramírez, Bee Ha Gan, Kaspar P. Locher, Jérémy Boilevin, Tamis Darbre, Daniel Janser, Markus Aebi, Jean-Louis Reymond, Rasomoy Biswas
Publikováno v:
Glycobiology
Glycobiology, 27 (6)
Ramírez, Ana S; Boilevin, Jérémy; Biswas, Rasomoy; Gan, Bee Ha; Janser, Daniel; Aebi, Markus; Darbre, Tamis; Reymond, Jean-Louis; Locher, Kaspar P (2017). Characterization of the single-subunit oligosaccharyltransferase STT3A from Trypanosoma brucei using synthetic peptides and lipid-linked oligosaccharide analogs. Glycobiology, 27(6), pp. 525-535. Oxford University Press 10.1093/glycob/cwx017
Glycobiology, 27 (6)
Ramírez, Ana S; Boilevin, Jérémy; Biswas, Rasomoy; Gan, Bee Ha; Janser, Daniel; Aebi, Markus; Darbre, Tamis; Reymond, Jean-Louis; Locher, Kaspar P (2017). Characterization of the single-subunit oligosaccharyltransferase STT3A from Trypanosoma brucei using synthetic peptides and lipid-linked oligosaccharide analogs. Glycobiology, 27(6), pp. 525-535. Oxford University Press 10.1093/glycob/cwx017
The initial transfer of a complex glycan in protein N-glycosylation is catalyzed by oligosaccharyltransferase (OST), which is generally a multisubunit membrane protein complex in the endoplasmic reticulum but a single-subunit enzyme (ssOST) in some p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9370a13b392269e784c0de07bf27257
http://doc.rero.ch/record/332115/files/GLYCOB_27_6_525.pdf
http://doc.rero.ch/record/332115/files/GLYCOB_27_6_525.pdf
Publikováno v:
Chemical Society Reviews
Bacterial infections caused by ‘superbugs’ are increasing globally, and conventional antibiotics are becoming less effective against these bacteria, such that we risk entering a post-antibiotic era. In recent years, antimicrobial peptides (AMPs)
A Study with Peptide Dendrimers Reveals an Extreme pH Dependence of Antibiotic Activity Above pH 7.4
In our efforts to develop peptide dendrimers as a new class of antimicrobial peptides (AMPs) against Gram-negative bacteria, we investigated their activity at acidic and basic pH, which correspond to the conditions of the site of bacterial infections
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3915b28738517f1d601b08acd6b459db
https://doi.org/10.26434/chemrxiv.14208287.v1
https://doi.org/10.26434/chemrxiv.14208287.v1
Publikováno v:
Chemical Communications (Cambridge, England)
Cai, Xingguang; Javor, Sacha; Gan, Bee Ha; Köhler, Thilo; Reymond, Jean-Louis (2021). The antibacterial activity of peptide dendrimers and polymyxin B increases sharply above pH 7.4. Chemical communications, 57(46), pp. 5654-5657. Royal Society of Chemistry 10.1039/D1CC01838H
Cai, Xingguang; Javor, Sacha; Gan, Bee Ha; Köhler, Thilo; Reymond, Jean-Louis (2021). The antibacterial activity of peptide dendrimers and polymyxin B increases sharply above pH 7.4. Chemical communications, 57(46), pp. 5654-5657. Royal Society of Chemistry 10.1039/D1CC01838H
pH-activity profiling reveals that antimicrobial peptide dendrimers (AMPDs) kill Klebsiella pneumoniae and Methicillin-resistant Staphylococcus aureus (MRSA) at pH = 8.0, against which they are inactive at pH = 7.4, due to stronger electrostatic bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2da42a6bb2414d9b58100b917406bec0
Publikováno v:
Chemical Society Reviews. 51:792-792
Correction for ‘The multifaceted nature of antimicrobial peptides: current synthetic chemistry approaches and future directions’ by Bee Ha Gan et al., Chem. Soc. Rev., 2021, 50, 7820–7880, DOI: 10.1039/D0CS00729C.
Autor:
Stéphane Baeriswyl, Sacha Javor, Christian van Delden, Ivan Di Bonaventura, Giovanni Di Bonaventura, Thissa N. Siriwardena, Jean-Louis Reymond, Alice Capecchi, Arianna Pompilio, Xian Jin, Thilo Köhler, Runze He, Bee Ha Gan
Publikováno v:
Chemical Communications, Vol. 54, No 40 (2018) pp. 5130-5133
We used the concept of chemical space to explore a virtual library of bicyclic peptides formed by double thioether cyclization of a precursor linear peptide, and identified an antimicrobial bicyclic peptide (AMBP) with remarkable activity against sev