446024-24-4Relevant academic research and scientific papers
Ring-deactivated hydroxyalkylpyrrole-based inhibitors of α-chymotrypsin: Synthesis and mechanism of action
Martyn, Derek C.,Vernall, Andrea J.,Clark, Bruce M.,Abell, Andrew D.
, p. 2103 - 2110 (2007/10/03)
13C NMR and mass spectrometry studies have been used to demonstrate that the inhibition of α-chymotrypsin by N-sulfonylhydroxymethylpyrrole inhibitors (10) is non-covalent. Hydroxyalkylpyrroles in which an electron-withdrawing group (acyl substituent) is introduced at the alternative C2 position have been synthesised and also shown to inactivate α-chymotrypsin. SAR studies on this class suggests that the incorporation of phenylalanine at C2 is favoured, however, there is little gain in introducing a hydrophobic substituent at C5.
An amino acid N-derivatising group that can be coloured on demand
Abell, Andrew D.,Martyn, Derek C.,May, Barnaby C.H.,Nabbs, Brent K.
, p. 3673 - 3675 (2007/10/03)
A method is presented whereby an amino acid is reacted with 5-formyl-1H-pyrrole-2-carboxylic acid to give an N-derivatised tag that has a latent ability to be coloured. A characteristic red pyrrolizin-3-one (coloured tag) is then revealed on treatment with hydrocinnamoyl chloride. This sequence has been carried out on amino acids in solution, and on solid phase, and also on dipeptides.
