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Molecular modeling aided design of nicotinic acid receptor GPR109A agonists.

Abstract：

:A homology model of the nicotinic acid receptor GPR109A was constructed based on the X-ray crystal structure of bovine rhodopsin. An HTS hit was docked into the homology model. Characterization of the binding pocket by a grid-based surface calculation of the docking model suggested that a larger hydrophobic body plus a polar tail would improve interaction between the ligand and the receptor. The designed compounds were synthesized, and showed significantly improved binding affinity and activation of GPR109A.

journal_name

Bioorg Med Chem Lett

journal_title

Bioorganic & medicinal chemistry letters

authors

Deng Q,Frie JL,Marley DM,Beresis RT,Ren N,Cai TQ,Taggart AK,Cheng K,Carballo-Jane E,Wang J,Tong X,Waters MG,Tata JR,Colletti SL

doi

10.1016/j.bmcl.2008.08.030

subject

Has Abstract

pub_date

2008-09-15 00:00:00

pages

4963-7

issue

18

eissn

0960-894X

issn

1464-3405

pii

S0960-894X(08)00952-9

journal_volume

18

pub_type

杂志文章

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