Tyrosinase inhibition: conformational analysis based studies on molecular dynamics calculations of bipiperidine based inhibitors.

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Khan KM, Saify ZS, Khan MT, Butt N, Maharvi GM, Perveen S, Ambreen N, Choudhary MI, Atta-Ur-Rahman, Supuran CT

Tyrosinase inhibition: conformational analysis based studies on molecular dynamics calculations of bipiperidine based inhibitors.

J Enzyme Inhib Med Chem. 2005 Aug;20(4):401-7.

PubMed ID

16206837 [ View in PubMed

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Abstract

Two series of variably N-substituted biperidines were synthesized by condensing various acid chlorides, alkyl halides and anhydrides with 1,4-bipiperidine. The new compounds were tested as tyrosinase inhibitors and a structure-activity relationship (SAR) study was carried out. Potent inhibition was observed in the case of the 4'-methylbenzyl substitution on this atom (IC50 = 1.72 microM) with this compound being a lead for future drug design. Additionally, calculations of the important QSAR molecular descriptors were done on the biperidine analogues after their 2 ps molecular dynamics (MD) simulations using molecular mechanics force field (MMFF) approaches. Using MD simulations potential and total energies were calculated for the energy minimized models of bipiperidine and the most active analogs 2, 3, 4, 6, 8 and 10.

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Binding Properties

Drug	Target	Property	Measurement	pH	Temperature (°C)
Mimosine	Tyrosinase	IC 50 (nM)	3.68E+03	6.8	37	Details