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).
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Boichot S,Krauss U,Plénat T,Rennert R,Milhiet PE,Beck-Sickinger A,Le Grimellec Cdoi
10.1016/j.febslet.2004.05.078keywords:
subject
Has Abstractpub_date
2004-07-02 00:00:00pages
346-50issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579304007227journal_volume
569pub_type
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