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

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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 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.
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