A native mass spectrometry approach to qualitatively elucidate interfacial epitopes of transient protein-protein interactions

被引：2

作者：

Veale, Clinton G. L. ^{[1
]}

Chakraborty, Abir ^{[2
]}

Mhlanga, Richwell ^{[2
]}

Albericio, Fernando ^{[3
]}

de la Torre, Beatriz G. ^{[4
]}

Edkins, Adrienne L. ^{[2
]}

Clarke, David J. ^{[5
]}

机构：

[1] Univ Cape Town, Dept Chem, ZA-7701 Cape Town, South Africa

[2] Rhodes Univ, Dept Biochem & Microbiol, Biomed Biotechnol Res Unit BioBRU, Makhanda, South Africa

[3] Univ KwaZulu Natal, Sch Chem & Phys, Westville, South Africa

[4] Univ KwaZulu Natal, Coll Hlth Sci, Sch Lab Med & Med Sci, Durban, South Africa

[5] Univ Edinburgh, EaStCHEM Sch Chem, Joseph Black Bldg,David Brewster Rd, Edinburgh EH9 3FJ, Scotland

来源：

CHEMICAL COMMUNICATIONS | 2024年 / 60卷 / 45期

基金：

英国生物技术与生命科学研究理事会;

关键词：

DOMAINS;

D O I：

10.1039/d4cc01251h

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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. Here we demonstrate a new approach in which native mass spectrometry and limited proteolysis is used in concert to rapidly identify interfacial peptides responsible for mediating a transient Protein-Protein Interaction.

引用

页码：5844 / 5847

页数：4

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