Differential binding of bispyridinium oxime drugs with acetylcholinesterase.

ABSTRACT:

Aim

To performe a time-dependent topographical delineation of protein-drug interactions to gain molecular insight into the supremacy of Ortho-7 over HI-6 in reactivating tabun-conjugated mouse acetylcholinesterase (mAChE).

Methods

We conducted all-atom steered molecular dynamics simulations of the two protein-drug complexes. Through a host of protein-drug interaction parameters (rupture force profiles, hydrogen bonds, water bridges, hydrophobic interactions), geometrical, and orientation ordering of the drugs, we monitored the enzyme's response during the release of the drugs from its active-site.

Results

The results show the preferential binding of the drugs with the enzyme. The pyridinium ring of HI-6 shows excellent complementary binding with the peripheral anionic

SUBMITTER: Kesharwani MK 

PROVIDER: S-EPMC4002407 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature