Leucine Aminopeptidase as a Target for Inhibitor Design

Authors: Grembecka J.; Kafarski P.

Source: Mini Reviews in Medicinal Chemistry, Volume 1, Number 2, July 2001 , pp. 133-144(12)

Publisher: Bentham Science Publishers

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Abstract:

In this review we focus on the most effective and the most promising inhibitors of leucine aminopeptidase. Their binding modes to the enzyme, the attempt to explain the origin of the inhibitory activity, as well as the structure - activity relationship for some of these compounds are discussed. Besides, the structural and electronic requirements of the enzyme active site and the binding pockets, together with the specificity towards the ligands, based on the structural and kinetic data, are presented.

Keywords: Inhibitor Design; inhibitors; leucine aminopeptidase; LAP aminoacyl-peptide hydrolase; LEUCINE AMINOPEPTIDASE INHIBITORS; Aminoaldehydes; Bestatin; Amastatin Analogues; AHPBA

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/1389557013406990

Publication date: 2001-07-01

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The aim of Mini-Reviews in Medicinal Chemistry is to publish short reviews on the important recent developments in medicinal chemistry and allied disciplines.

The scope of Mini-Reviews in Medicinal Chemistry will cover all areas of medicinal chemistry including developments in rational drug design, synthetic chemistry, bioorganic chemistry, high-throughput screening, combinatorial chemistry, drug targets, and natural product research and structure-activity relationship studies.

Mini-Reviews in Medicinal Chemistry is an essential journal for every medicinal and pharmaceutical chemist who wishes to be kept informed and up-to-date with the latest and most important developments.