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Updated: Aug 24, 2026

Measuring Peptide Translocation into Large Unilamellar Vesicles
Published on: January 27, 2012
Molecular mechanism of Peptide-induced pores in membranes
Huey W Huang1, Fang-Yu Chen, Ming-Tao Lee
1Department of Physics & Astronomy, Rice University, Houston, Texas 77251, USA.
Abstract:
We suggest a physical mechanism by which antimicrobial peptides spontaneously induce stable pores in membranes. Peptide binding to a lipid bilayer causes an internal stress, or internal membrane tension, that can be sufficiently strong to create pores. Like detergents, peptides have a high affinity for the rim of the pore. Binding to the rims reduces the line tension and decreases the number of peptides causing the internal membrane tension. Consequently, the pore radius is stable. The pore formation resembles a phase transition.
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