effect of disulfide bridges deletion on the conformation of the androctonin, polyphemusin-i, and thanatin antimicrobial peptides molecular dynamics simulation studies二硫桥删除效果的构象androctonin,polyphemusin-i,thanatin抗菌肽分子动力学模拟研究.pdfVIP
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effect of disulfide bridges deletion on the conformation of the androctonin, polyphemusin-i, and thanatin antimicrobial peptides molecular dynamics simulation studies二硫桥删除效果的构象androctonin,polyphemusin-i,thanatin抗菌肽分子动力学模拟研究
Vol.2, No.3, 244-257 (2011) Journal of Biophysical Chemistry
doi:10.4236/jbpc.2011.23030
Effect of disulfide bridges deletion on the
conformation of the androctonin, polyphemusin-I,
and thanatin antimicrobial peptides: molecular
dynamics simulation studies
*
Jorge Ricardo Moreira Castro , Carlos Alessando Fuzo, Léo Degrève
Grupo de Simulação Molecular, Faculdade de Filosofia Ciências e Letras de Ribeirão Preto, Universidade de São Paulo,
*
Ribeirão Preto, Brazil; Corresponding Author: jrcastro@usp.br
Received 6 March 2011; revised 27 April 2011; accepted 15 May 2011.
ABSTRACT ever, nature itself has endowed some organisms with
antimicrobial peptides, which are distinctive tools for
In this work, the role of the disulfide bridges in survival [8]. In this context, the production of antimicro-
the maintenance of the secondary structure of bial peptides is a powerful evolutionary ancient defen-
the antimicrobial peptides androctonin, poly- sive weapon [9] that allows living organisms like plants,
phemusin-I, and thanatin is analyzed on the ba- vertebrate and invertebrate animals, as well as fungi and
sis of their structural characteristics and of bacteria to survive. Many organisms make use of antim-
three of their respective mutants, andry4, poly4, icrobial peptides to defend themselves against harmful
and thany2, in which all the cysteine residues invader microorganisms. These peptides are part of the
have been replaced with tyrosine residue
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