K. Priya

Bio: K. Priya is an academic researcher. The author has contributed to research in topics: Primary alcohol & Pyranose. The author has an hindex of 2, co-authored 3 publications receiving 13 citations.

β-1- N -Acetamido- D -glucopyranose

Abstract: In the title molecule, C 8 H 15 NO 6 , the pyranose ring adopts the usual 4 C 1 (D) conformation and the N-acetyl group exists in the Z-anti conformation. The orientation of the primary alcohol group is gauche.

β-1-N-Benzamido-d-glucopyranose

Abstract: In the title compound, 1-benzamido-β-d-glucopyranose, C13H17NO6, the pyranose ring adopts the 4C1(D) conformation and the N-acetyl group exists in the Z-anti conformation. The primary alcohol group is disordered between the two permitted orientations, gg and gt.

β-1-N-Benzamido-D-glucopyranose.

Abstract: In the title compound, 1-benzamido-β-d-glucopyranose, C13H17NO6, the pyranose ring adopts the 4C1(D) conformation and the N-acetyl group exists in the Z-anti conformation. The primary alcohol group is disordered between the two permitted orientations, gg and gt.

Crystallographic and computational studies on 4‐phenyl‐N‐(β‐D‐glucopyranosyl)‐1H‐1,2,3‐triazole‐1‐acetamide, an inhibitor of glycogen phosphorylase: Comparison with α‐D‐glucose, N‐acetyl‐β‐D‐glucopyranosylamine and N‐benzoyl‐N′‐β‐D‐glucopyranosyl urea binding

Abstract: 4-Phenyl-N-(beta-D-glucopyranosyl)-1H-1,2,3-triazole-1-acetamide (glucosyltriazolylacetamide) has been studied in kinetic and crystallographic experiments with glycogen phosphorylase b (GPb), in an effort to utilize its potential as a lead for the design of potent antihyperglycaemic agents Docking and molecular dynamics (MD) calculations have been used to monitor more closely the binding modes in operation and compare the results with experiment Kinetic experiments in the direction of glycogen synthesis showed that glucosyltriazolylacetamide is a better inhibitor (K(i) = 018 mM) than the parent compound alpha-D-glucose (K(i) = 17 mM) or beta-D-glucose (K(i) = 74 mM) but less potent inhibitor than the lead compound N-acetyl-beta-D-glucopyranosylamine (K(i) = 32 microM) To elucidate the molecular basis underlying the inhibition of the newly identified compound, we determined the structure of GPb in complex with glucosyltriazolylacetamide at 100 K to 188 A resolution, and the structure of the compound in the free form Glucosyltriazolylacetamide is accommodated in the catalytic site of the enzyme and the glucopyranose interacts in a manner similar to that observed in the GPb-alpha-D-glucose complex, while the substituent group in the beta-position of the C1 atom makes additional hydrogen bonding and van der Waals interactions to the protein A bifurcated donor type hydrogen bonding involving O3H, N3, and N4 is seen as an important structural motif strengthening the binding of glucosyltriazolylacetamide with GP which necessitated change in the torsion about C8-N2 bond by about 62 degrees going from its free to the complex form with GPb On binding to GP, glucosyltriazolylacetamide induces significant conformational changes in the vicinity of this site Specifically, the 280s loop (residues 282-288) shifts 07 to 31 A (CA atoms) to accommodate glucosyltriazolylacetamide These conformational changes do not lead to increased contacts between the inhibitor and the protein that would improve ligand binding compared with the lead compound In the molecular modeling calculations, the GOLD docking runs with and without the crystallographic ordered cavity waters using the GoldScore scoring function, and without cavity waters using the ChemScore scoring function successfully reproduced the crystallographic binding conformation However, the GLIDE docking calculations both with (GLIDE XP) and without (GLIDE SP and XP) the cavity water molecules were, impressively, further able to accurately reproduce the finer details of the GPb-glucosyltriazolylacetamide complex structure The importance of cavity waters in flexible receptor MD calculations compared to "rigid" (docking) is analyzed and highlighted, while in the MD itself very little conformational flexibility of the glucosyltriazolylacetamide ligand was observed over the time scale of the simulations

Observation of a unique pattern of bifurcated hydrogen bonds in the crystal structures of the N-glycoprotein linkage region models.

Abstract: Elucidation of the intra- and intermolecular carbohydrate-protein interactions would greatly contribute toward obtaining a better understanding of the structure-function correlations of the protein-linked glycans. The weak interactions involving C-H...O have recently been attracting immense attention in the domain of biomolecular recognition. However, there has been no report so far on the occurrence of C-H...O hydrogen bonds in the crystal structures of models and analogs of N-glycoproteins. We present herein an analysis of C-H...O interactions in the crystal structures of all N-glycoprotein linkage region models and analogs. The study reveals a cooperative network of bifurcated hydrogen bonds consisting of N-H...O and C-H...O interactions seen uniquely for the models. The cooperative network consists of two antiparallel chains of bifurcated hydrogen bonds, one involving N1-H, C2'-H and O1' of the aglycon moiety and the other involving N2-H, C1-H and O1'' of the sugar. Such bifurcated hydrogen bonds between the core glycan and protein are likely to play an important role in the folding and stabilization of proteins.

Crystallographic Studies on α- and β-D-glucopyranosyl Formamide Analogues, Inhibitors of Glycogen Phosphorylase

Abstract: The catalytic site of glycogen phosphorylase (GP) is currently under investigation as a target for inhibition of hepatic glycogenolysis under high glucose conditions. Three D-glucopyranosyl analogues, C-(1-azido-α-D-glucopyranosyl) formamide, C-(1-acetamido-α-D-glucopyranosyl) formamide, and C-(1-hydroxy-β-D-glucopyranosyl) formamide, were recognised as moderate competitive inhibitors of muscle glycogen phosphorylase b (GPb) [with respect to α-D-glucose 1-phosphate (Glc-1-P)] with Ki values of 1.80 (±0.2) mM, 0.31 (±0.01) mM, and 0.88 (±0.04) mM, respectively. In order to elucidate the structural basis of inhibition, we determined the structure of muscle GPb complexed with the three compounds at 2.1, 2.06 and 2.0 A resolution, respectively. The complex structures revealed that the inhibitors can be accommodated in the catalytic site of T-state GPb with very little change of the tertiary structure, and provide a rationalisation for understanding potency of the inhibitors. The glucopyranose moiety m...