四肽的分子重组:探索主链酯化在阴离子结合中的作用。

IF 2.9 2区 化学 Q3 CHEMISTRY, PHYSICAL
Monalisha Sarma, Manabendra Sarma
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引用次数: 0

摘要

了解生物分子和阴离子之间的相互作用在生物化学和环境科学中是至关重要的。沉积肽是一种类似肽,其中一个或多个酰胺键被酯键取代,与常规肽相比具有更大的灵活性和改变的结合特性。在这项研究中,我们利用构象采样、分子动力学模拟和电子结构计算,探索了甘氨酸基四磷酸肽作为磷酸二氢(H2PO4-)和硫酸氢(HSO4-)在气相和水相中的受体。发现酯键的位置会影响成键的几何形状和能量学。O─H·O = C和N─H·O = O等氢键相互作用是稳定受体-阴离子配合物的主要驱动力,非共价相互作用(NCI)指数支持了这一点。在溶液中,水分子与受体竞争阴离子结合,从而影响相互作用强度和配合物的几何形状。这些结果表明,肽骨架中的酯取代可以作为设计有效的肽基阴离子受体的有效策略。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Molecular Rewiring of Tetrapeptides: Exploring the Role of Backbone Esterification in Anion Binding.

Understanding the interactions between biomolecules and anions is crucial in biochemistry and environmental science. Depsipeptide, a peptide analogue in which one or more amide bonds are replaced with ester linkages, provides greater flexibility and altered binding properties compared to regular peptides. In this study, we explored a glycine-based tetradepsipeptide as a receptor for dihydrogen phosphate (H2PO4-) and hydrogen sulfate (HSO4-) using conformational sampling, molecular dynamics simulations, and electronic structure calculations in both gas and aqueous phases. The position of ester linkages was found to influence the geometry and energetics of binding. Hydrogen bonding interactions such as O─H···O═C and N─H···O were the main driving force that stabilized the receptor-anion complexes, as supported by the noncovalent interaction (NCI) index. In solution, water molecules compete with the receptor for anion binding, thereby influencing both the interaction strength and the geometry of the complexes. These results show that ester substitution in peptide backbones can be a useful strategy for designing effective peptide-based anion receptors.

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来源期刊
CiteScore
5.80
自引率
9.10%
发文量
965
审稿时长
1.6 months
期刊介绍: An essential criterion for acceptance of research articles in the journal is that they provide new physical insight. Please refer to the New Physical Insights virtual issue on what constitutes new physical insight. Manuscripts that are essentially reporting data or applications of data are, in general, not suitable for publication in JPC B.
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