Effect of β-O-glucosylation on L-Ser and L-Thr diamides:: A bias toward α-helical conformations

被引:34
|
作者
Corzana, Francisco
Busto, Jesus H.
Engelsen, Soren B.
Jimenez-Barbero, Jesus
Asensio, Juan L.
Peregrina, Jesus M.
Avenoza, A. [1 ]
机构
[1] Univ La Rioja, Dept Quim, CSIC, UA, Logrono 26006, Spain
[2] Royal Vet & Agr Univ, DK-1958 Frederiksberg C, Denmark
[3] CSIC, E-28040 Madrid, Spain
[4] CSIC, Inst Quim Organ, E-28006 Madrid, Spain
关键词
conformation analysis; glycopeptides; molecular dynamics; NMR spectroscopy; peptides;
D O I
10.1002/chem.200600128
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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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页码:7864 / 7871
页数:8
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