Calcitonin-derived carrier peptide plays a major role in the membrane localization of a peptide-cargo complex

FEBS Letters
Sylvie BoichotChristian Le Grimellec

Abstract

Bilayers made of dioleoylphosphatidylcholine (DOPC)/dipalmitoylphosphatidylcholine (DPPC) mixture containing or not cholesterol (Chl) were used to investigate the interaction of a carrier peptide with membranes. Atomic force microscopy revealed that the C-terminal 9-32 fragment of human calcitonin (hCT (9-32)), free or coupled to enhanced green fluorescent protein (hCT-eGFP) cargo forms aggregates in the DOPC fluid phase in absence of Chl and in the DPPC enriched liquid-ordered phase when Chl is present. The data show that hCT (9-32) plays a determinant role in the membrane localization of the peptide-cargo complex. They suggest that carpet-like mechanism for membrane destabilization may be involved in the carrier function of hCT (9-32).

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Citations

Mar 30, 2007·European Biophysics Journal : EBJ·Daniela MeleleoSilvia Micelli
Dec 28, 2007·Advanced Drug Delivery Reviews·Robert RennertAnnette G Beck-Sickinger
Apr 20, 2007·Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology·José Roberto S A LeiteCarlos Bloch
Oct 4, 2005·Biophysical Journal·Thomas PlénatChristian Le Grimellec
Oct 3, 2009·Biochimica Et Biophysica Acta·Marie-Cécile GiocondiChristian Le Grimellec

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