Lead modification: amino acid appended indoles as highly effective 5-LOX inhibitors

Parteek Prasher; Pooja; Palwinder Singh

doi:10.1016/j.bmc.2014.01.027

Lead modification: amino acid appended indoles as highly effective 5-LOX inhibitors

Bioorg Med Chem. 2014 Mar 1;22(5):1642-8. doi: 10.1016/j.bmc.2014.01.027. Epub 2014 Jan 29.

Authors

Parteek Prasher¹, Pooja¹, Palwinder Singh²

Affiliations

¹ Department of Chemistry, Guru Nanak Dev University, Amritsar 143005, India.
² Department of Chemistry, Guru Nanak Dev University, Amritsar 143005, India. Electronic address: palwinder_singh_2000@yahoo.com.

PMID: 24508141
DOI: 10.1016/j.bmc.2014.01.027

Abstract

N-1 tosyl indoles carrying amino acid as a part of C-3 substituent are identified with considerable 5-LOX inhibitory activities. On the basis of enzyme inhibitory activities and logP, it is found that these compounds are more suitable to use as ester prodrugs. In addition to the significant Ka and Ki for 5-LOX, advantageously the compounds under present investigation do not affect the viability of the cell. The experimental results were also supported by molecular docking of compounds in the active site of 5-LOX.

Keywords: 5-LOX inhibition; Amino acid; Indole; Molecular modeling.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acids
Indoles / pharmacology*
Lipoxygenase Inhibitors / pharmacology*
Models, Molecular
Molecular Docking Simulation
Structure-Activity Relationship

Substances

Amino Acids
Indoles
Lipoxygenase Inhibitors