96289-13-3Relevant articles and documents
The Wittig bioconjugation of maleimide derived, water soluble phosphonium ylides to aldehyde-tagged proteins
Asbjarnarson, Arni,Gudjonsson, Thorarinn,Hartmann, Rafael W.,Helgudottir, Hildur Run,Lehmann, Fredrik,Nilvebrant, Johan,Nygren, Per-?ke,Odell, Luke R.,Pijnappel, Matthijs,Traustadottir, Gunnhildur Asta
supporting information, p. 10417 - 10423 (2021/12/17)
Herein we disclose the transformation of maleimides into water-soluble tris(2-carboxyethyl)phosphonium ylides and their subsequent application in the bioconjugation of protein- and peptide-linked aldehydes. The new entry into Wittig bioconjugate chemistry proceeds under mild conditions and relies on highly water soluble reagents, which are likely already part of most biochemists' inventory. This journal is
Glycopolypeptides with a redox-triggered helix-to-coil transition
Kramer, Jessica R.,Deming, Timothy J.
, p. 4112 - 4115 (2012/04/10)
Conformation-switchable glycopolypeptides were prepared by the living polymerization of glycosylated l-cysteine-N-carboxyanhydride (glyco-C NCA) monomers. These new monomers were prepared in high yield by coupling of alkene-terminated C-linked glycosides of d-galactose or d-glucose to l-cysteine using thiol-ene "click" chemistry, followed by their conversion to the corresponding glyco-C NCAs. The resulting glycopolypeptides were found to be water-soluble and α-helical in solution. Aqueous oxidation of the side-chain thioether linkages in these polymers to sulfone groups resulted in disruption of the α-helical conformations without loss of water solubility. The ability to switch chain conformation and remain water-soluble is unprecedented in synthetic polymers, and allows new capabilities to control presentation of sugar functionality in subtly different contexts.
Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase
Bounaga, Sakina,Galleni, Moreno,Laws, Andrew P,Page, Michael I
, p. 503 - 510 (2007/10/03)
Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-β-lactamase. The pH dependence of pKi indicates that the thiol anion displaces hydroxide ion from the active site zinc(II). D,D-Peptides bind to the enzyme better than other diastereoisomers, which is compatible with the predicted stereochemistry of the active site.