特异性多肽在半导体基底上粘附的微观机理
Microscopic Mechanism of Specific Peptide Adhesion to Semiconductor Substrates
摘要：
为纳米技术应用如生物分子纳米阵列设计混合肽-固体界面需要深入了解肽在固体基质上结合和组装的基本机制。在这里，我们通过实验和计算分析表明，突变的合成肽在半导体上的吸附特性表现出明显的序列依赖性粘附特异性。我们的模拟一种新的混合肽基板模型揭示了脯氨酸突变和结合亲和力之间的对应关系，以一个干净的硅基板。在合成理论上建议的具有不同结合行为的氨基酸序列后，我们在随后的原子力显微镜实验中证实了粘附时选择性突变的相关性。
英文摘要：
The design of hybrid peptide-solid interfaces for nanotechnological applications such as biomolecular nanoarrays requires a deep understanding of the basic mechanisms of peptide binding and assembly at solid substrates. Here we show by means of experimental and computational analyses that the adsorption properties of mutated synthetic peptides at semiconductors exhibit a clear sequence-dependent adhesion specificity. Our simulations of a novel hybrid peptide-substrate model reveal the correspondence between proline mutation and binding affinity to a clean silicon substrate. After synthesizing theoretically suggested amino-acid sequences with different binding behavior, we confirm the relevance of the selective mutations upon adhesion in our subsequent atomic force microscopy experiments.
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