Yang, Tangpo published the artcileA bifunctional amino acid to study protein-protein interactions, Name: (4-Bromobut-1-yn-1-yl)trimethylsilane, the publication is RSC Advances (2020), 10(69), 42076-42083, database is CAplus and MEDLINE.
Protein-protein interactions (PPIs) play crucial roles in regulating essentially all cellular processes. Photo-crosslinking 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-crosslinking, 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.
RSC Advances published new progress about 69361-41-7. 69361-41-7 belongs to bromides-buliding-blocks, auxiliary class PROTAC Linker,Aliphatic Linker, name is (4-Bromobut-1-yn-1-yl)trimethylsilane, and the molecular formula is C11H8F2, Name: (4-Bromobut-1-yn-1-yl)trimethylsilane.
Referemce:
https://en.wikipedia.org/wiki/Bromide,
bromide – Wiktionary