AI Article Synopsis
- Researchers studied bilayers made from a mixture of two types of phosphatidylcholine (DOPC and DPPC) to see how a specific peptide interacts with membranes.
- Atomic force microscopy revealed that a fragment of human calcitonin (hCT (9-32)), either on its own or attached to a protein, forms aggregates in certain lipid phases depending on the presence of cholesterol.
- The findings suggest that hCT (9-32) is crucial for how the peptide-cargo complex is positioned in membranes and may destabilize membranes through a "carpet-like" mechanism to aid in its carrier function.
Article 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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| http://dx.doi.org/10.1016/j.febslet.2004.05.078 | DOI Listing |
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