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Role of acetylation and charge in antimicrobial peptides based on human β‐defensin‐3
Author(s) -
PAPANASTASIOU EMILIOS ANDREW,
HUA QUYEN,
SANDOUK ALINE,
SON U HYON,
CHRISTENSON ANDREW JAMES,
VAN HOEK MONIQUE LOUISE,
BISHOP BARNEY MICHAEL
Publication year - 2009
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1111/j.1600-0463.2009.02460.x
Subject(s) - antimicrobial , antimicrobial peptides , defensin , beta defensin , peptide , innate immune system , chemistry , escherichia coli , acetylation , potency , microbiology and biotechnology , biochemistry , biology , in vitro , gene , receptor
Cationic antimicrobial peptides are an evolutionarily ancient and essential element of innate immunity in higher organisms. The precise mechanism by which these peptides exert their antimicrobial activity on bacteria is not well understood. Decapeptides based on the C‐terminus of human β‐defensin‐3 were designed and evaluated to study the role of charge in defining the antimicrobial activity and selectivity of these peptides against Escherichia coli . Acetylated derivatives of these peptides were prepared in order to further evaluate how positively charged primary amines contribute to potency in these small antimicrobial peptides. These peptides enabled us to explore the relationship between net charge, charge distribution and antimicrobial activity. While the results indicate that net charge is a major factor in antimicrobial activity in these peptides, the actual relationship between charge and potency appears to be more complex.