A substantial body of work has been carried out describing the structural features of the complex between single-domain antibodies (VHHs) and antigens, and the preeminence for epitopes located at concave surfaces of the antigen. However, the thermodynamic basis of binding is far less clear. Here, we have analysed the energetic profiles of five VHHs binding to the catalytic cleft or to a noncleft epitope of hen egg lysozyme. Various binding energetic profiles with distinctive enthalpic/entropic contributions and structural distribution of critical residues were found in the five antibodies analysed. Collectively, we suggest that from an energetic point of view the binding mechanism is influenced by the shape of the epitope. This information may be beneficial for the design of tailored epitopes for VHHs and their practical use.

中文翻译：

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针对鸡蛋溶菌酶的单域抗体的表位依赖性热力学特征

已经进行了大量的工作来描述单域抗体 (VHH) 和抗原之间的复合物的结构特征，以及位于抗原凹面的表位的优势。然而，结合的热力学基础远不那么清楚。在这里，我们分析了与催化裂隙或鸡蛋溶菌酶的非裂隙表位结合的五种 VHH 的能量分布。在分析的五种抗体中发现了具有独特焓/熵贡献和关键残基结构分布的各种结合能量分布。总的来说，我们建议从能量的角度来看，结合机制受表位形状的影响。该信息可能有助于为 VHH 设计定制的表位及其实际应用。