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非经典非共价 σ-孔相互作用在蛋白质结构和功能中的应用:潜在蛋白质工程应用的概念。

Non-classical Non-covalent σ-Hole Interactions in Protein Structure and Function: Concepts for Potential Protein Engineering Applications.

机构信息

Department of Biochemistry & Molecular Biology, 1870 Campus Delivery, Colorado State University, Fort Collins, CO, 80523-1870, USA.

出版信息

Chem Asian J. 2023 Apr 3;18(7):e202300026. doi: 10.1002/asia.202300026. Epub 2023 Feb 24.

DOI:10.1002/asia.202300026
PMID:36764929
Abstract

The structures and associated functions of biological molecules are driven by noncovalent interactions, which have classically been dominated by the hydrogen bond (H-bond). Introduction of the σ-hole concept to describe the anisotropic distribution of electrostatic potential of covalently bonded elements from across the periodic table has opened a broad range of nonclassical noncovalent (ncNC) interactions for applications in chemistry and biochemistry. Here, we review how halogen bonds, chalcogen bonds and tetrel bonds, as they are found naturally or introduced synthetically, affect the structures, assemblies, and potential functions of peptides and proteins. This review intentionally focuses on examples that introduce or support principles of stability, assembly and catalysis that can potentially guide the design of new functional proteins. These three types of ncNC interactions have energies that are comparable to the H-bond and, therefore, are now significant concepts in molecular recognition and design. However, the recently described H-bond enhanced X-bond shows how synergism among ncNC interactions can be exploited as potential means to broaden the range of their applications to affect protein structures and functions.

摘要

生物分子的结构和相关功能是由非共价相互作用驱动的,这些相互作用传统上主要由氢键(H-bond)主导。将σ-hole 概念引入描述整个元素周期表中共价键合元素的静电势各向异性分布,为化学和生物化学中的应用开辟了广泛的非经典非共价(ncNC)相互作用。在这里,我们回顾了卤键、硫键和碲键,以及它们在自然界中发现或人工引入时如何影响肽和蛋白质的结构、组装和潜在功能。本综述有意侧重于介绍或支持稳定性、组装和催化原理的例子,这些原理可能有助于指导新功能蛋白的设计。这三种类型的 ncNC 相互作用的能量与 H-bond 相当,因此,它们现在是非共价相互作用识别和设计的重要概念。然而,最近描述的 H-bond enhanced X-bond 表明,ncNC 相互作用之间的协同作用如何可以被利用为潜在的手段来扩大它们的应用范围,以影响蛋白质的结构和功能。

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