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Updated: Aug 1, 2026

Measuring Peptide Translocation into Large Unilamellar Vesicles
Published on: January 27, 2012
Translocation of protegrin I through phospholipid membranes: role of peptide folding
Guillaume Drin1, Jamal Temsamani
1Synt:em, Parc Scientifique Georges Besse, 3000 Nîmes, France. gdrin@syntem.com
Abstract:
The protegrin PG-1, belonging to the family of beta-stranded antimicrobial peptides, exerts its activity by forming pores in the target biological membranes. Linear analogues derived from PG-1 do not form pores in the phospholipid membranes and have been used successfully to deliver therapeutic compounds into eucaryotic cells. In this paper, the translocation of PG-1 and of a linear analogue through artificial phospholipid membranes was investigated, leading to a possible mechanism for the activity of these peptidic vectors. We report here that [12W]PG-1, a fluorescent analogue of PG-1, is able to translocate through lipid bilayers and we demonstrate that this property depends on its secondary structure. Our results agree with the recent mechanism proposed for the translocation and permeabilisation activities of several helical and beta-stranded peptides. In addition, our data corroborate recent work suggesting that certain protegrin-derived vectors enter into endothelial cells by adsorptive-mediated endocytosis.
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