1338593-99-9Relevant academic research and scientific papers
Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links
Haney, Conor M.,Loch, Matthew T.,Horne, W. Seth
, p. 10915 - 10917 (2011)
Covalent side-chain cross-linking has been shown to be a viable strategy to control peptide folding. We report here that an oxime side-chain linkage can elicit α-helical folds from peptides in aqueous solution. The bio-orthogonal bridge is formed rapidly
