NDLI: Effect of Repetitive Lysine-Tryptophan Motifs on the Eukaryotic Membrane

Content Provider	PubMed Central
Author	Gopal, Ramamourthy Lee, Jong Kook Lee, Jun Ho Kim, Young Gwon Chae, Oh Gwang Seo, Chang Ho Park, Yoonkyung
Copyright Year	2013
Abstract	In a previous study, we synthesized a series of peptides containing simple sequence repeats, (KW) n –NH2 (n = 2,3,4 and 5) and determined their antimicrobial and hemolytic activities, as well as their mechanism of antimicrobial action. However, (KW)5 showed undesirable cytotoxicity against RBC cells. In order to identify the mechanisms behind the hemolytic and cytotoxic activities of (KW)5, we measured the ability of these peptides to induce aggregation of liposomes. In addition, their binding and permeation activities were assessed by Trp fluorescence, calcein leakage and circular dichrorism using artificial phospholipids that mimic eukaryotic liposomes, including phosphatidylcholine (PC), PC/sphingomyelin (SM) (2:1, w/w) and PC/cholesterol (CH) (2:1, w/w). Experiments confirmed that only (KW)5 induced aggregation of all liposomes; it formed much larger aggregates with PC:CH (2:1, w/w) than with PC or PC:SM (2:1, w/w). Longer peptide (KW)5, but not (KW)3 or (KW)4, strongly bound and partially inserted into PC:CH compared to PC or PC:SM (2:1, w/w). Calcein release experiments showed that (KW)5 induced calcein leakage from the eukaryotic membrane. Greater calcein leakage was induced by (KW)5 from PC:CH than from PC:SM (2:1, w/w) or PC, whereas (KW)4 did not induce calcein leakage from any of the liposomes. Circular dichroism measurements indicated that (KW)5 showed higher conformational transition compared to (KW)4 due to peptide-liposome interactions. Taken together, our results suggest that (KW)5 reasonably mediates the aggregation and permeabilization of eukaryotic membranes, which could in turn explain why (KW)5 displays efficient hemolytic activity.
Related Links	http://dx.doi.org/10.3390/ijms14012190
Ending Page	2202
Page Count	13
Starting Page	2190
File Format	PDF
ISSN	14220067
e-ISSN	14220067
Journal	International Journal of Molecular Sciences
Issue Number	1
Volume Number	14
Language	English
Publisher	MDPI
Publisher Date	2013-01-01
Access Restriction	Open
Rights Holder	MDPI
Subject Keyword	Physical and Theoretical Chemistry Inorganic Chemistry Organic Chemistry Spectroscopy Molecular Biology Catalysis Computer Science Applications Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Organic Chemistry Medicine Molecular Biology Physical and Theoretical Chemistry Catalysis Inorganic Chemistry Computer Science Applications

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