Epitope-dependent thermodynamic signature of single-domain antibodies against hen egg lysozyme

Autor:	Hiroki Akiba, Jose M. M. Caaveiro, Kouhei Tsumoto, Hiroko Tamura
Rok vydání:	2021
Předmět:	biology Chemistry General Medicine Single-Domain Antibodies Surface Plasmon Resonance Crystallography X-Ray Biochemistry Epitope Structural distribution Epitopes Antigen Hen Egg Lysozyme Biophysics biology.protein Animals Thermodynamics Muramidase Antibody Chickens Molecular Biology Protein Binding
Zdroj:	The Journal of Biochemistry. 170:623-629
ISSN:	1756-2651 0021-924X
DOI:	10.1093/jb/mvab082
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3e803e739f1fcdeef0e747b57ba69d5 https://doi.org/10.1093/jb/mvab082 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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