Hydrophobic Residues Confer the Helicity and Membrane Permeability of Ocellatin-1 Antimicrobial Peptide Scaffold Towards Therapeutics
Author:
Funder
vit university
Publisher
Springer Science and Business Media LLC
Subject
Drug Discovery,Molecular Medicine,Biochemistry,Bioengineering,Analytical Chemistry
Link
https://link.springer.com/content/pdf/10.1007/s10989-021-10265-1.pdf
Reference48 articles.
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3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H et al (2000) The protein data bank. Nucleic Acids Res 28(1):235–242
4. Chandrasekhar G, Rajasekaran R (2020) Investigating the pernicious effects of heparan sulfate in serum amyloid A1 protein aggregation: a structural bioinformatics approach. J Biomol Struct Dyn. https://doi.org/10.1080/07391102.2020.1833756
5. Chen Y, Guarnieri MT, Vasil AI, Vasil ML, Mant CT, Hodges RS (2007) Role of peptide hydrophobicity in the mechanism of action of α-helical antimicrobial peptides. Antimicrob Agents Chemother 51(4):1398–1406
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