BTTAA
Description
Application Data
Description
-
BTTAA is an optimised water-soluble ligand for the copper(I)-catalysed azide-alkyne cycloaddition (CuAAC) to significantly accelerate rate kinetics of bioorthogonal reactions without effecting cell cytotoxicity.
Application Data
-
Catalogue number crb7108431 Molecular Weight 430.52 Chemical Composition C19H30N10O2 Appearance Off-white to grey solid Solubility Water, DMSO, DMF, MeOH Chemistry Acid Purity >95% cas 1334179-85-9 Storage 4°C Manufacturer Product Number 1236 Citations Wood, T. M., et al., (2021). Optimization of Metabolic Oligosaccharide Engineering with Ac4GalNAlk and Ac4GlcNAlk by an Engineered Pyrophosphorylase. ACS Chem. Biol., 16(10): 1961. https://doi.org/10.1021/acschembio.1c00034.
Yang et al., (2014). Biocompatible click chemistry enabled compartment-specific pH measurement inside E. coli. Nat. Commun., 5(1): 1. DOI: 10.1038/ncomms5981.
References Wood, T. M., et al., (2021). Optimization of Metabolic Oligosaccharide Engineering with Ac4GalNAlk and Ac4GlcNAlk by an Engineered Pyrophosphorylase. ACS Chem. Biol., 16(10): 1961. https://doi.org/10.1021/acschembio.1c00034.
Yang et al., (2014). Biocompatible click chemistry enabled compartment-specific pH measurement inside E. coli. Nat. Commun., 5(1): 1. DOI: 10.1038/ncomms5981.
Click chemistry CuAAC is used in vitro successfully for conjugation, immobilization, and purification of biomolecules. However, bioorthogonal labelling of cytoplasmic molecules has remained elusive due to a high background. Furthermore, the copper moiety was too toxic till the advent of the latest generation of ligands. BTTAA has been successfully used in Click chemistry to allow in situ labelling of E. coli compartmentalised proteins without apparent cytotoxicity. In mammalian cells, BTTAA with CuAAC were used to aid in protein labelling on the surface of living cells producing a vastly higher signal than with previous ligands used. As a localisation method, BTTAA CuAAC reactions were utilised to help enrich the glycoprotein of gut bacteria Bacteroides fragilis and Parabacteroides distasonis. Click chemistry generated a detectable glycoprotein biophysical probe to help understand the peptide’s role in host colonisation. The applications for BTTAA in Click chemistry in bioorthogonal reactions are being uncovered with each piece of research and continue to surpass its predecessors.