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Calcitonin‐derived carrier peptide plays a major role in the membrane localization of a peptide–cargo complex
Author(s) -
Boichot Sylvie,
Krauss Ulrike,
Plénat Thomas,
Rennert Robert,
Milhiet Pierre-Emmanuel,
Beck-Sickinger Annette,
Le Grimellec Christian
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.05.078
Subject(s) - dipalmitoylphosphatidylcholine , peptide , membrane , biophysics , chemistry , calcitonin , target peptide , phospholipid , biochemistry , biology , phosphatidylcholine , endocrinology
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).