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作 者:LI JiHong DANG QinQin SUN HongWei CHA RuiTao YUAN Zhi
机构地区:[1]College of Chemistry, Nankai University, Tianjin 300071, China [2]College of Basic Medical Science, Tianjin Medical University, Tianjin 300070, China [3]College of Material Science and Chemical Engineering, Tianjin University of Science and Technology, Tianjin 300457, China
出 处:《Chinese Science Bulletin》2008年第3期473-476,共4页
基 金:the National Natural Science Foundation of China(Grant Nos.50573034 and 20634030)
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.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 peptides, 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 o-helix conformation of V8. So the ad- sorption capacity of DMAPAM to V8 was higher. This was significant to explore the interaction mechanism between peptides and biomaterials.
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