Structural & Conformational Characterstics of Tilted Peptides: Role of Hydrophobicity in Structural & Conformational Characterstics of Tilted Peptides (Prolactin & Growth Hormone)

Tilted peptides are short helical peptides (11 to 20 aa long), known to destabilize membranes and lipid cores. These 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, due to an asymmetric distribution of hydrophobic residues along the axis of the ?-helix, Such peptides adopt an oblique orientation which can destabilize membranes or lipid cores. Tilted peptides of Prolactin (PRL) and Growth hormone (GH) have attracted immense amount of researches in their structure and their characterstics studies because of their special functional properties: inhibition of angiogenesis, inhibition of endothelial cell proliferation and induce endothelial cell apoptosis.