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Cross-Linking Furan-Modified Kisspeptin-10 to the KISS Receptor.

Abstract：

:Chemical cross-linking is well-established for investigating protein-protein interactions. Traditionally, photo cross-linking is used but is associated with problems of selectivity and UV toxicity in a biological context. We here describe, with live cells and under normal growth conditions, selective cross-linking of a furan-modified peptide ligand to its membrane-presented receptor with zero toxicity, high efficiency, and spatio-specificity. Furan-modified kisspeptin-10 is covalently coupled to its glycosylated membrane receptor, GPR54(KISS1R). This newly expands the applicability of furan-mediated cross-linking not only to protein-protein cross-linking but also to cross-linking in situ. Moreover, in our earlier reports on nucleic acid interstrand cross-linking, furan activation required external triggers of oxidation (via addition of N-bromo succinimide or singlet oxygen). In contrast, we here show, for multiple cell lines, the spontaneous endogenous oxidation of the furan moiety with concurrent selective cross-link formation. We propose that reactive oxygen species produced by NADPH oxidase (NOX) enzymes form the cellular source establishing furan oxidation.

journal_name

ACS Chem Biol

journal_title

ACS chemical biology

authors

Vannecke W,Ampe C,Van Troys M,Beltramo M,Madder A

doi

10.1021/acschembio.7b00396

subject

Has Abstract

pub_date

2017-08-18 00:00:00

pages

2191-2200

issue

8

eissn

1554-8929

issn

1554-8937

journal_volume

12

pub_type

杂志文章

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