Abstract
Caveolin‐1 and ‐3 are among the few proteins in which the functional domains are contiguous and modular. The interaction of synthetic peptides spanning the scaffolding domain of caveolin‐3 with model membranes has been investigated. The peptides include the scaffolding domain, the aromatic and positively charged residues at the C‐terminal end of this domain as well as deletion of three amino acids TFT, observed in certain patients with limb girdle muscular dystrophy. All of the peptides appear to be peripherally bound to the bilayer surface. However, no preferential binding to sphingomyelin and cholesterol‐containing lipid vesicles was observed. Deletion of TFT appears to affect the association with lipid vesicles compared with the native sequence. Association with lipids decreases considerably when TFT as well as the aromatic‐rich segment YWFYR, which occurs at the extreme C‐terminus of the scaffolding domain, are deleted. © 2006 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 615–624, 2006
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