Structural Determinants of the Unusual Helix Stability of a De Novo Engineered Vascular Endothelial Growth Factor (VEGF) Mimicking Peptide

Helix stability: Understanding helix stability and formation is a prerequisite to elucidate the mechanism of protein folding and design helix peptides with specific activity. Herein, we analyze the thermal behaviour of a designed, -helical, bioactive peptide, composed only of natural amino acids. This peptide shows an unusual thermal stability, in which the N-terminal region and a hydrophobic interaction play a major role (see figure).