Design of serine protease inhibitors with conformation restricted by amino acid side-chain-side-chain CH/π interaction

A novel type of conformationally restricted peptides with the structure of H–D‐Xaa–Phe–NH–CH2–C6H5 has been developed as inhibitors of serine proteinase chymotrypsin. The D‐Xaa–alkyl and Phe–phenyl groups resulted in a formation of the hydrophobic core due to the side‐chain–side‐chain CH/π interacti...

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Veröffentlicht in:	BIOPOLYM 1999, Vol.51 (1), p.9-17
Hauptverfasser:	Shimohigashi, Yasuyuki, Nose, Takeru, Yamauchi, Yasuko, Maeda, Iori
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids Catalyst activity CH/π interaction chymotrypsin conformational restriction Conformations Crystallography enzyme inhibitor Hydrophobicity inhibitory conformation Molecular dynamics Molecular structure
Online-Zugang:	Volltext
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