1280729-83-0Relevant academic research and scientific papers
Affinity of aporphines for the human 5-HT2A receptor: Insights from homology modeling and molecular docking studies
Pecic, Stevan,Makkar, Pooja,Chaudhary, Sandeep,Reddy, Boojala V.,Navarro, Hernan A.,Harding, Wayne W.
, p. 5562 - 5575 (2010)
Analogs of nantenine were docked into a modeled structure of the human 5-HT2A receptor using ICM Pro, GLIDE, and GOLD docking methods. The resultant docking scores were used to correlate with observed in vitro apparent affinity (Ke) data. The GOLD docking algorithm when used with a homology model of 5-HT2A, based on a bovine rhodopsin template and built by the program MODELLER, gives results which are most in agreement with the in vitro results. Further analysis of the docking poses among members of a C1 alkyl series of nantenine analogs, indicate that they bind to the receptor in a similar orientation, but differently than nantenine. Besides an important interaction between the protonated nitrogen of the C1 alkyl analogs and residue Asp155, we identified Ser242, Phe234, and Gly238 as key residues responsible for the affinity of these compounds for the 5-HT2A receptor. Specifically, the ability of some of these analogs to establish a H-bond with Ser242 and hydrophobic interactions with Phe234 and Gly238 appears to explain their enhanced affinity as compared to nantenine.
Nantenine as an acetylcholinesterase inhibitor: SAR, enzyme kinetics and molecular modeling investigations
Pecic, Stevan,McAnuff, Marie A.,Harding, Wayne W.
experimental part, p. 46 - 55 (2011/10/13)
Nantenine, as well as a number of flexible analogs, were evaluated for acetylcholinesterase (AChE) inhibitory activity in microplate spectrophotometric assays based on Ellman'a€s method. It was found that the rigid aporphine core of nantenine is an import
