Calcitonin-derived carrier peptide plays a major role in the membrane localization of a peptide-cargo complex.
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).
Boichot
Sylvie
S
Nanostructures et Complexes Membranaires, C.B.S. CNRS UMR5048-INSERM U554, 29 rue de Navacelles, 34090 Montpellier Cedex, France.
Krauss
Ulrike
U
Plénat
Thomas
T
Rennert
Robert
R
Milhiet
Pierre-Emmanuel
PE
Beck-Sickinger
Annette
A
Le Grimellec
Christian
C
D000595:Amino Acid Sequence; D002116:Calcitonin / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D049452:Green Fluorescent Proteins; D006801:Humans; D007700:Kinetics; D008051:Lipid Bilayers / Q000378:metabolism*; D008164:Luminescent Proteins / Q000378:metabolism; D008563:Membrane Lipids / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000378:metabolism
D002352:Carrier Proteins; D008051:Lipid Bilayers; D008164:Luminescent Proteins; D008563:Membrane Lipids; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins; D002116:Calcitonin