Probing the molecular mechanisms of quartz-binding peptides.
Probing the molecular mechanisms of quartz-binding peptides.
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DOI：
10.1021/la100049s
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发表时间：
2010-07
期刊：
影响因子：
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通讯作者：
E. Oren;R. Notman;I. Kim;J. Evans;T. Walsh;R. Samudrala;C. Tamerler;M. Sarikaya
中科院分区：
文献类型：
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作者：
E. Oren;R. Notman;I. Kim;J. Evans;T. Walsh;R. Samudrala;C. Tamerler;M. Sarikaya
了解生物矿化机制和实现受生物学启发的无机材料形成很大程度上取决于我们操纵肽/固体界面相互作用的能力。材料界面和生物界面是生物无机合成、表面扩散和分子识别的关键部位。最近采用的生物组合技术允许分离识别无机固体的肽，这些无机固体用作分子构建块，例如作为合成器、接头和组装器。尽管它们在纳米技术、生物技术和医学中无处不在，但工程肽与无机表面结合的分子识别的基本机制仍然很大程度上未知。为了探索连接在肽/固体相互作用中发挥关键作用的序列、结构和功能的倾向规则，我们结合了两种不同的方法：在从头设计的肽中搜索高度丰富的基序的统计分析，以及三种经过实验验证的肽的原子模拟。选择两种强石英结合肽和一种弱石英结合肽在含水条件下模拟石英 (100) 表面。通过圆二色性测量分析基于溶液的肽结构。小而疏水的残基，例如 Pro，通过与固体紧密接触并阻碍肽内氢键的形成，在界面上发挥关键作用。肽的高结合亲和力可以由有利的焓效应和熵效应的组合驱动，即，强结合物可以拥有大量可能的结合构型，其中许多具有相对高的结合能。结果表明局部分子环境在参与固体结合的关键残基中的作用。本文的工作描述了材料特异性肽固有的分子构象，并提供了对肽/固体界面的原子理解的基本见解。
Understanding the mechanisms of biomineralization and the realization of biology-inspired inorganic materials formation largely depends on our ability to manipulate peptide/solid interfacial interactions. Material interfaces and biointerfaces are critical sites for bioinorganic synthesis, surface diffusion, and molecular recognition. Recently adapted biocombinatorial techniques permit the isolation of peptides recognizing inorganic solids that are used as molecular building blocks, for example, as synthesizers, linkers, and assemblers. Despite their ubiquitous utility in nanotechnology, biotechnology, and medicine, the fundamental mechanisms of molecular recognition of engineered peptides binding to inorganic surfaces remain largely unknown. To explore propensity rules connecting sequence, structure, and function that play key roles in peptide/solid interactions, we combine two different approaches: a statistical analysis that searches for highly enriched motifs among de novo designed peptides, and, atomistic simulations of three experimentally validated peptides. The two strong and one weak quartz-binding peptides were chosen for the simulations at the quartz (100) surface under aqueous conditions. Solution-based peptide structures were analyzed by circular dichroism measurements. Small and hydrophobic residues, such as Pro, play a key role at the interface by making close contact with the solid and hindering formation of intrapeptide hydrogen bonds. The high binding affinity of a peptide may be driven by a combination of favorable enthalpic and entropic effects, that is, a strong binder may possess a large number of possible binding configurations, many of which having relatively high binding energies. The results signify the role of the local molecular environment among the critical residues that participate in solid binding. The work herein describes molecular conformations inherent in material-specific peptides and provides fundamental insight into the atomistic understanding of peptide/solid interfaces.