Open AccessEffect of degree of unsaturation of fatty acids on the activity of FabI (enoyl-acyl carrier protein reductase) enzyme from Plasmodium falciparum: an enzoinformatics study
Author(s) -
Sibhghatulla Shaikh,
Syed Mohd Danish Rizvi,
Rashmi Tripathi,
Deboshree Biswas,
Shazi Shakil
Publication year - 2014
Publication title -
asian pacific journal of tropical disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.208
H-Index - 33
ISSN - 2222-1808
DOI - 10.1016/s2222-1808(14)60717-9
Subject(s) - degree of unsaturation , docosahexaenoic acid , biochemistry , polyunsaturated fatty acid , enzyme , fatty acid , reductase , chemistry , arachidonic acid , stereochemistry , organic chemistry
Objective: To elucidate molecular interactions of enoyl-acyl carrier protein reductase (FabI)\udwith unsaturated fatty acids such as docosahexaenoic acid, eicosapentaenoic acid, arachidonic\udacid, octadecatrienoic acid, stearic acid and arachic acid to investigate the inhibitory activities of\uddegree of unsaturation.\udMethods: Docking between these ligands and enzymes were performed using Autodock4.2.\udResults: Docosahexaenoic acid (a polyunsaturated fatty acid) is more efficient inhibitor of enoylacyl carrier protein reductase (FabI) compared to other unsaturated fatty acids with lesser double\udbonds and saturated fatty acid with reference to ∆G and Ki values. Hydrophobic interactions play\udan important role in the correct positioning of these fatty acids within the catalytic site of FabI\udenzyme to permit docking.\udConclusions: It has been also observed that not only the degree of unsaturation affects the\udantiplasmodial activity, but the length of carbon chain also plays an important role in their\udinhibitory activity. Such information may aid in the design of versatile FabI-inhibitors