一种用于定性阐明瞬时蛋白-蛋白相互作用界面表位的本地质谱方法。
A native mass spectrometry approach to qualitatively elucidate interfacial epitopes of transient protein-protein interactions.
机构信息
Department of Chemistry, University of Cape Town, Rondebosch, Cape Town 7701, South Africa.
The Biomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry and Microbiology, Rhodes University, Makhanda, South Africa.
出版信息
Chem Commun (Camb). 2024 May 30;60(45):5844-5847. doi: 10.1039/d4cc01251h.
Native mass spectrometric analysis of TPR2A and GrpE with unpurified peptides derived from limited proteolysis of their respective PPI partners (HSP90 C-terminus and DnaK) facilitated efficient, qualitative identification of interfacial epitopes involved in transient PPI formation. Application of this approach can assist in elucidating interfaces of currently uncharacterised transient PPIs.
利用未经纯化的肽段（分别来自 HSP90 C 端和 DnaK 与 TPR2A 和 GrpE 的部分酶解产物）进行天然质谱分析，有助于高效、定性地鉴定瞬时蛋白质-蛋白质相互作用形成过程中涉及的界面表位。该方法的应用有助于阐明目前尚未明确的瞬时蛋白质-蛋白质相互作用界面。
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