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Effect of cholesterol on the membrane interaction of Modelin-5 isoforms.

Abstract：

:Modelin-5 isoforms were used to gain an insight into the effects of amidation on antimicrobial selectivity. When tested against Escherichia coli, amidation increased toxicity 10-fold (MIC = 31.25 μM) while showing limited increased hemolytic activity (2% lysis). Our results show that both the amidated and non-amidated peptides had a disordered structure in aqueous solution (<18% helical) and folded to form helices at the membrane interface (for example, >43% in the presence of DMPC). The stabilization of the helical structure by amidation has previously been shown to play a key role in increasing antibacterial efficacy. The presence of cholesterol in the membrane increases the packing density (C(s)(-1) values 25-33 mN m(-1)) and so prevents the peptide from forming stable association with the membrane, which is evidenced by the higher binding coefficient (K(d)) in the presence of cholesterol: 57.70 μM for Modelin-5-COOH and 35.64 μM for Modelin-5-CONH(2) compared to the presence of E. coli lipid extract (10 μM), which would prevent local concentration of the peptide at the bilayer interface as seen by reduction in monolayer interaction. This in turn would be predicted to inhibit activity.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Dennison SR,Phoenix DA

doi

10.1021/bi201267v

subject

Has Abstract

pub_date

2011-12-20 00:00:00

pages

10898-909

issue

50

eissn

0006-2960

issn

1520-4995

journal_volume

50

pub_type

杂志文章

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