Effect of disulfide bridges deletion on the conformation of the androctonin, polyphemusin-I, and thanatin antimicrobial peptides: molecular dynamics simulation studies

Autor:	Fuzo Carlos Alessando, Degrève Léo, Castro Jorge Ricardo Moreira
Rok vydání:	2011
Předmět:	Molecular dynamics Stereochemistry Hydrogen bond Chemistry Antimicrobial peptides Mutant Aromaticity Tyrosine Protein secondary structure Cysteine
Zdroj:	Journal of Biophysical Chemistry. :244-257
ISSN:	2153-0378 2153-036X
DOI:	10.4236/jbpc.2011.23030
Popis:	In this work, the role of the disulfide bridges in the maintenance of the secondary structure of the antimicrobial peptides androctonin, poly-phemusin-I, and thanatin is analyzed on the basis of their structural characteristics and of three of their respective mutants, andry4, poly4, and thany2, in which all the cysteine residues have been replaced with tyrosine residues. The absence of the disulfide bridges in andry4, poly4, and thany2 seems to be compensated by an overall enforcement of the original hydrogen bonds and by extra attractive interactions between the aromatic rings of the tyrosine residues. In spite of the mutations, the original β-hairpin structures are maintained in the three mutants, but the best conformational similarities are found for the androctonin/andry4 pair.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::fb4eff397e0887e5eb050be8fdba79cb https://doi.org/10.4236/jbpc.2011.23030 Zobrazit plný text záznamu