Tilted peptides

Tilted peptides, called also oblique-oriented peptides, are short helical peptide sequences (11 to 20 amino acids long) that are characterized by a peculiar distribution of hydrophobic residues: they are amphipathic and their net hydrophobicity increases from one end of the helix to the other (Thomas and Brasseur, 2006; Harris et al, 2006). These hydrophobicity gradients allow the alpha-helices to penetrate the membrane at a shallow angle, thereby destabilising membrane lipid organisation and promoting a range of biological processes. Tilted peptides show little sequence homology, but a common feature is their ability to induce liposome fusion in vitro (Pillot et al, 1996).

Nguyen et al (2006) have reported that several tilted peptide sequences can inhibit angiogenesis. This involves inhibition of ... ... ... ...
 
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Entry last modified: December 2011