Effect of beta-O-glucosylation on L-Ser and L-Thr diamides: a bias toward alpha-helical conformations.
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.
Corzana
Francisco
F
Departamento de Química, Universidad de La Rioja UA-CSIC. 26006 Logroño, Spain.
Busto
Jesús H
JH
Engelsen
Søren B
SB
Jiménez-Barbero
Jesús
J
Asensio
Juan L
JL
Peregrina
Jesús M
JM
Avenoza
A
A
D002236:Carbohydrate Conformation; D003958:Diamide / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D005947:Glucose / Q000378:metabolism*; D006020:Glycopeptides / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012694:Serine / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics; D013912:Threonine / Q000737:chemistry* / Q000378:metabolism
D006020:Glycopeptides; D003958:Diamide; D013912:Threonine; D012694:Serine; D005947:Glucose