纤维形成多肽表面吸附与折叠的竞争
The competition between surface adsorption and folding of fibril-forming polypeptides
摘要：
多肽自组装成纤维状结构可以由与某些残基有利地相互作用的平面表面引发。使用粗粒模型，我们系统地研究了$β$ -辊成型多肽的折叠和吸附行为。我们发现，有两种不同的折叠途径取决于温度：（i）在低温下，多肽折叠成$β$ -卷在溶液中吸附到有吸引力的表面上之前，（ii）在较高的温度下，多肽首先吸附在一个无序的状态，折叠，而在表面上。折叠温度随着吸引力的增加而增加，因为折叠的$β$ -辊被表面稳定。令人惊讶的是，进一步增加吸引力再次降低折叠温度，因为强吸引力也稳定了吸附的无序状态，这与多肽的折叠竞争。我们的研究结果表明，为了增强折叠，应该使用弱吸引表面。他们还解释了最近实验观察到的电荷对相反电荷表面上原纤维形成的非单调效应[C。Charbonneau等人，ACS Nano，8，2328（2014）]。
英文摘要：
Self-assembly of polypeptides into fibrillar structures can be initiated by planar surfaces that interact favorably with certain residues. Using a coarse grained model, we systematically studied the folding and adsorption behavior of a $β$-roll forming polypeptide. We find that there are two different folding pathways depending on the temperature: (i) at low temperature, the polypeptide folds in solution into a $β$-roll before adsorbing onto the attractive surface, (ii) at higher temperature, the polypeptide first adsorbs in a disordered state, and folds while on the surface. The folding temperature increases with increasing attraction, as the folded $β$-roll is stabilized by the surface. Surprisingly, further increasing the attraction lowers the folding temperature again, as strong attraction also stabilizes the adsorbed disordered state, which competes with folding of the polypeptide. Our results suggest that to enhance the folding, one should use a weakly attractive surface. They also explain the recent experimental observation of the non-monotonic effect of charge on the fibril formation on an oppositely charged surface [C. Charbonneau, et al., ACS Nano, 8, 2328 (2014)].
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