Pharmacophore-based structure optimization of angiotensin converting enzyme inhibitory peptide

• 来源期刊: 中国科学B辑（英文版）
• 年，卷（期）: 2008,（8）
• 页码范围: 786-793
• 页数: 8页
• 语种: 英文
• DOI: 10.1007/s 11426-008-0085-5

摘要

Chemical feature based pharmacophore models were generated for an angiotensin converting enzyme (ACE) inhibitory peptide using the Discovery Studio 2.0 pharmacophore modeling approach. The pharmacophore hypothesis selected has five features (one negative lonizable region, one hydrogen bond donor, one hydrogen bond acceptor and two hydrophobic functional groups). Additionally, ACE inhibitory hexapeptide previously obtained from silkworm pupae protein was optimized to target the ACE based on the selected pharmacophore. The results suggest that tri-peptide (thr-val-phe) may be structural determinant of ACE activity. Docking studies further provided confidence for the validity of the selected pharmacophore model to perform structure optimization of the ACE inhibitory peptide.