The effect of α-helix comformation on interaction between model oligopeptides and polymers

• 来源期刊: 科学通报（英文版）
• 年，卷（期）: 2008,（3）
• 页码范围: 473-476
• 页数: 4页
• 语种: 英文
• DOI: 10.1007/s11434-008-0065-3

摘要

The study of interactions between peptides and synthetic polymers has aroused considerable interest recently. In the present paper, the interaction mechanism between adsorbent DMAPAM and two pep-tides, VVRGCTWW(V8) and CTWW(C4), was investigated at molecular level by NMR and molecular stimulation. The results demonstrated that the conformation of oligopeptides played a vital role in their adsorption capacity on the adsorbent. Weak interactions could incorporate with each other between V8 and DMAPAM because there was a hydrophobic cleavage in α-helix conformation of V8. So the ad-sorption capacity of DMAPAM to V8 was higher. This was significant to explore the interaction mecha-nism between peptides and biomaterials.