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• W2027835544 abstract "Reversibly associating peptides present an attractive strategy for the intracellular delivery and release of therapeutic compounds or polynucleotides. We have explored the efficacy of the small, cysteine-containing heptapeptide (KL)3C for model membrane disruption. The peptide can reversibly dimerize via cysteine oxidation and cystine reduction; the differing redox potentials inside and outside cells should stabilize the dimeric form extracellularly, and the monomeric form intracellularly. The peptide did not show detectable permeabilization activity with zwitterionic phosphatidylcholine (PC) vesicles, but was active toward anionic (fatty-acid-containing) vesicles with either phosphatidylethanolamine or PC lipids. In all cases, the dimeric form of the peptide was more active than the monomer, at equal concentrations. Binding measurements show that the dimer binds much more strongly to the anionic membranes than does the monomer, but quantitative fitting suggests that this is due almost entirely to a greater charge on the dimer (which concentrates the peptide near the membrane surface), rather than to its increased hydrophobicity. Correlation between membrane binding and leakage rates shows that the membrane destabilization does not require peptide cooperativity. Moreover, the effectiveness of bound dimer is not higher than that of bound monomer: the greater efficacy of the dimer is thus a consequence of its increased binding. These model membrane studies show that cysteine-mediated dimerization is a useful approach to controlling membrane properties in an environment-sensitive manner." @default.
• W2027835544 created "2016-06-24" @default.
• W2027835544 creator A5000419225 @default.
• W2027835544 creator A5042152649 @default.
• W2027835544 date "2003-02-01" @default.
• W2027835544 modified "2023-09-27" @default.
• W2027835544 title "Effects of oxidation and reduction on the membrane activity of a cysteine dimerizable peptide" @default.
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• W2027835544 doi "https://doi.org/10.1016/s0927-7765(02)00068-1" @default.
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