A bifunctional amino acid to study protein-protein interactions.
Journal
RSC advances
ISSN: 2046-2069
Titre abrégé: RSC Adv
Pays: England
ID NLM: 101581657
Informations de publication
Date de publication:
17 Nov 2020
17 Nov 2020
Historique:
received:
25
10
2020
accepted:
12
11
2020
entrez:
6
5
2022
pubmed:
18
11
2020
medline:
18
11
2020
Statut:
epublish
Résumé
Protein-protein interactions (PPIs) play crucial roles in regulating essentially all cellular processes. Photo-cross-linking represents a powerful method to study PPIs. To fulfil the requirements for the exploration of different PPIs, there is a continuous demand on the development of novel photo-reactive amino acids with diverse structural properties and functionalities. Reported herein is the development of a bifunctional amino acid termed dzANA, which contains a diazirine, for photo-cross-linking, and a terminal alkyne group, for bioorthogonal tagging. Using known PPIs between histone posttranslational modifications (PTMs) and their binding partners as models, we demonstrate that the dzANA-harbouring peptide-based photoaffinity probes could efficiently and selectively capture the weak and transient PPIs mediated by histone modifications. Our study indicates the potential of dzANA to identify and characterize unknown PPIs.
Identifiants
pubmed: 35516754
doi: 10.1039/d0ra09110c
pii: d0ra09110c
pmc: PMC9057919
doi:
Types de publication
Journal Article
Langues
eng
Pagination
42076-42083Informations de copyright
This journal is © The Royal Society of Chemistry.
Déclaration de conflit d'intérêts
There are no conflicts to declare.
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