Antimicrobial Peptides and Their Interactions with Model Membranes

Rzeszutek, Agnieszka; Willumeit, R.

doi:10.1016/b978-0-12-381266-7.00006-7

Cited by 2 publications

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“…NK-lysin was isolated from porcine small intestine and displays cytotoxic and antimicrobial activity [ 25 ]. The sequence of NK-2 has been used as a template to design new derivatives with improved activity and to understand the relevance of structural and physicochemical peptide features such as α-helicity, charge and amphipathicity for the interactions with the membrane of pathogens [ 28 , 29 ]. NKCS was derived from NK-2 by replacement of the cysteine at position 7 by serine, what yielded a more stable peptide, which is resistant to oxidation.…”

Section: Introductionmentioning

confidence: 99%

NKCS, a Mutant of the NK-2 Peptide, Causes Severe Distortions and Perforations in Bacterial, But Not Human Model Lipid Membranes

et al. 2015

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NKCS is an improved mutant of the bioactive peptide NK-2, which shows strong activity against Escherichia coli and low toxicity towards human cells. The different activity demonstrates the relevance of the physico-chemical nature of the target membrane for the biological effect of this peptide. We studied the effect of this potent antimicrobial peptide on model membranes by activity studies, differential scanning calorimetry, single molecule tracking and tracer efflux experiments. We found that NKCS severely distorted, penetrated and perforated model lipid membranes that resembled bacterial membranes, but not those that were similar to human cell membranes. The interactions of NKCS with phosphatidylethanolamine, which is abundant in bacterial membranes, were especially strong and are probably responsible for its antimicrobial activity.

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Section: Introductionmentioning

confidence: 99%