680622-68-8

Usage

Chemical Properties

Off-White Solid

InChI:InChI=1/C10H15N6.ClH/c1-16(4-2-3-5-16)9-7-8(13-6-12-7)14-10(11)15-9;/h6H,2-5H2,1H3,(H3,11,12,13,14,15);1H/q+1;/p-1

Upstream product

• 120-94-5 1-Methylpyrrolidine 
• 10310-21-1 2-Amino-6-chloropurin 
• 10310-21-1 2-amino-6-chloropurine 

Downstream Products

• 1151762-33-2 6-((4-(azidomethyl)benzyl)oxy)-9H-purin-2-amine 
• 680622-70-2 N-[ [4-[(2-amino-7H-purin-6-yl)oxymethyl]phenyl]methyl]-2,2,2-trifluoroacetamide 
• 680622-70-2 N-[4-(2-amino-9H-purin-6-yloxymethyl)benzyl]-2,2,2-trifluoroacetamide 
• 1055972-12-7 N-[2-(2-amino-9H-purin-6-yloxymethyl)benzyl]-2,2,2-trifluoroacetamide 
• 1055972-09-2 N-(3-(((2-amino-9H-purin-6-yl)oxy)methyl)benzyl)-2,2,2-trifluoroacetamide 

Relevant academic research and scientific papers

Photoproximity Profiling of Protein-Protein Interactions in Cells

We report a novel photoproximity protein interaction (PhotoPPI) profiling method to map protein-protein interactions in vitro and in live cells. This approach utilizes a bioorthogonal, multifunctional chemical probe that can be targeted to a genetically encoded protein of interest (POI) through a modular SNAP-Tag/benzylguanine covalent interaction. A first generation photoproximity probe, PP1, responds to 365 nm light to simultaneously cleave a central nitroveratryl linker and a peripheral diazirine group, resulting in diffusion of a highly reactive carbene nucleophile away from the POI. We demonstrate facile probe loading, and subsequent interaction- A nd light-dependent proximal labeling of a model protein-protein interaction (PPI) in vitro. Integration of the PhotoPPI workflow with quantitative LC-MS/MS enabled unbiased interaction mapping for the redox regulated sensor protein, KEAP1, for the first time in live cells. We validated known and novel interactions between KEAP1 and the proteins PGAM5 and HK2, among others, under basal cellular conditions. By contrast, comparison of PhotoPPI profiles in cells experiencing metabolic or redox stress confirmed that KEAP1 sheds many basal interactions and becomes associated with known lysosomal trafficking and proteolytic proteins like SQSTM1, CTSD, and LGMN. Together, these data establish PhotoPPI as a method capable of tracking the dynamic subcellular and protein interaction "social network" of a redox-sensitive protein in cells with high temporal resolution.

A β-chloro ethylnitrosourea compound and its synthetic method and use

The invention relates to novel beta-chloroethylnitrosourea compounds, and a synthesis method and application thereof. The structure of the beta-chloroethylnitrosourea compounds is disclosed as general formula (II). The in-vitro antitumor screening test on the compounds disclosed as general formula II proves that the compounds disclosed as general formula I have obvious inhibiting action on human cerebral nerve glioma cells SF763, SF767, SF126 and SF188, human colon cancer cell HT29, mouse leukaemia cell L1210 and many other tumor cell lines and have higher tumor inhibiting activity than the existing CENU and CENU/O6-benzylguanine combined medicine.

Highly activatable and environment-insensitive optical highlighters for selective spatiotemporal imaging of target proteins

Optical highlighters are photoactivatable fluorescent molecules that exhibit pronounced changes in their spectral properties in response to irradiation with light of a specific wavelength and intensity. Here, we present a novel design strategy for a new class of caged BODIPY (4,4-difluoro-4-bora-3a, 4a-diaza-s-indacene) fluorophores, based on the use of photoremovable protecting groups (PRPGs) with high reduction potentials that serve as both a photosensitive unit and a fluorescence quencher via photoinduced electron transfer (PeT). 2,6-Dinitrobenzyl (DNB)-caged BODIPY was efficiently photoactivated, with activation ratios exceeding 600-fold in aqueous solutions. We then combined this photoactivatable fluorophore with a SNAP (mutant of O 6-alkylguanine DNA alkyltransferase) ligand to obtain a small-molecule-based optical highlighter for visualization of protein dynamics, using the well-established SNAP tag technology. As proof of concept, we demonstrate spatiotemporal imaging of the fusion protein of epidermal growth factor receptor (EGFR) with SNAP tag in living cells. We also demonstrate highlighting of cells of interest in live zebrafish embryos, using the fusion protein of histone 2A with SNAP tag.

One- and two-photon live cell imaging using a mutant SNAP-Tag protein and its FRET substrate pairs

A small molecule-assisted protein labeling strategy based on a mutant SNAP-Tag (mSNAP) and its FRET substrate pairs has been developed. Both one- and two-photon fluorescence microscopic experiments were successfully demonstrated in living cells.