What question did this study set out to answer?

To determine how ring size, structure, and amphipathicity of Gramicidin S-derived cyclic cationic peptides influence their conformation and mode of interaction with neutral and negatively charged lipid bilayers.

July 1, 2002Journal of Peptide Research

Conformation and interaction of the cyclic cationic antimicrobial peptides in lipid bilayers

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Authors

MJMasoud Jelokhani‐NiarakiWilfrid Laurier University EPElmar J. PrennerUniversity of Calgary CKC.M. KayNew Mexico State University

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Implication

In vitro study reveals membrane charge and peptide structure drive lipid bilayer disruption, suggesting antimicrobial activity depends on distinct hydrophobic and electrostatic mechanisms.

Key Points

To determine how ring size, structure, and amphipathicity of Gramicidin S-derived cyclic cationic peptides influence their conformation and mode of interaction with neutral and negatively charged lipid bilayers.
Evaluated four cyclic peptides (GS10, GS12, GS14, and [d-Lys]4GS14) across neutral (PC) and negatively charged (PE/PG) micelles and phospholipid vesicles.
Employed circular dichroism and fluorescence spectroscopy alongside ultracentrifugation to characterize peptide secondary structure, insertion depth, and membrane binding.
Assayed membrane permeabilization by monitoring the release of entrapped fluorescent dye from unilamellar vesicles.
Hydrophobic interactions served as the dominant driver for peptide insertion into zwitterionic PC vesicles and directly correlated with hemolytic activity.
Peptide-induced vesicle aggregation and membrane fusion in negatively charged PE/PG bilayers occurred through combined electrostatic and hydrophobic forces with potency decreasing in the order: [d-Lys]4GS14 > GS14 > GS12 > GS10.
Peptide insertion depth varied by structure, with GS10 and GS14 inserting deeply toward the hydrophobic membrane core, whereas GS12 and [d-Lys]4GS14 positioned near the outer interfacial boundary.

Cite This Study

Jelokhani‐Niaraki et al. (2002) studied this question.

synapsesocial.com/papers/6a8fe2d52c8afd1913414548 https://doi.org/10.1034/j.1399-3011.2002.21003.x

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Implication

In vitro study reveals membrane charge and peptide structure drive lipid bilayer disruption, suggesting antimicrobial activity depends on distinct hydrophobic and electrostatic mechanisms.

Conformation and interaction of the cyclic cationic antimicrobial peptides in lipid bilayers

Discussion

Member takes

Implication

Key Points

Cite This Study

Conformation and interaction of the cyclic cationic antimicrobial peptides in lipid bilayers

Discussion

Member takes

Implication

Key Points

Cite This Study

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