Molecular modelling studies on the binding of some protides to the putative human phosphoramidase Hint1.
The aim of the present work is to investigate through molecular modelling the possible role of the human enzyme Hint1 in the final P-N bond cleavage of phosphoramidate ProTides, which would lead to the intracellular delivery of unmasked nucleoside analogue monophosphates. Herein, we report our preliminary analysis based on docking studies of (E)-5-(2-bromovinyl)-2'-deoxyuridine (BVdU) related aminoacyl phosphates with Hint1 and the effect of the amino acid moiety on the enzyme-substrate binding affinity.
Welsh School of Pharmacy, Cardiff University, Cardiff, United Kingdom. sphcc3@cf.ac.uk
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Congiatu
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Brancale
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McGuigan
D000577:Amides / Q000378:metabolism*; D001973:Bromodeoxyuridine / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism; D020134:Catalytic Domain; D006801:Humans; D008958:Models, Molecular; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000378:metabolism*; D010756:Phosphoric Acids / Q000378:metabolism*; D011487:Protein Conformation; D013379:Substrate Specificity
D000577:Amides; C063306:HINT1 protein, human; D009419:Nerve Tissue Proteins; D010756:Phosphoric Acids; C020235:brivudine; C011067:phosphoramidic acid; D001973:Bromodeoxyuridine