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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Effect of beta-O-glucosylation on L-Ser and L-Thr diamides: a bias toward alpha-helical conformations
Francisco Corzana1, Jesús H Busto, Søren B Engelsen
1Departamento de Química, Universidad de La Rioja UA-CSIC. 26006 Logroño, Spain.
Abstract:
Beta-D-O-glucosylation produces a remarkable effect on the peptide backbone of the model peptides derived from serine and threonine. Consequently, this type of glycosylation is responsible for the experimentally observed shift from extended conformations (model peptides) towards the folded conformations (model glycopeptides). The conclusion has been solidly assessed by a combined NMR/MD protocol. Interestingly, the MD (molecular dynamics) results for the glycopeptides point towards the existence of water-bridging molecules between the sugar and peptide moieties, which could explain the stabilization of the folded conformers in aqueous solution.
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