International Journal of Biochemistry and Biotechnology

Full Length Research Paper

Structural features in neuropsin as potential target for pharmacological inhibition in brain diseases

Reinaldo Barros Geraldo^1,4, Paula Campello Costa Lopes²,  Carlos Rangel Rodrigues³, Russolina Benedeta Zingali⁴ _, Helena C. Castro ¹

¹Antibiotics Laboratory, Biochemistry, and Molecular Modeling Study (LABioMol), Department of Molecular Cell Biology, Institute of Biology, CEG - Universidade Federal Fluminense, Rio de Janeiro, Brazil.

²Neural Neuroplasticity Laboratory, Department of Neurobiology, Institute of Biology, CEG - Universidade Federal Fluminense, Rio de Janeiro, Brazil.

³Laboratory of Molecular Modeling and QSAR (ModmolQSAR), Faculty of Pharmacy, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.

⁴Institute of Medical Biochemistry, Structural Biology Program, CCS, UFRJ, CEP 21941-590, Rio de Janeiro, RJ, Brazil.

 *Corresponding author: E-mail:[email protected].

Accepted 21 February, 2013

Abstract

Neuropsin is a serine-protease produced by neurons and glial cells that is directly involved in learning and memory processes. This enzyme presents an important role in brain diseases such as epilepsy and Alzheimer disease. In this work we reviewed several aspects about this enzyme including structure, biological activity and its role in the central nervous system. We also compared neuropsin with other serine-proteases such as trypsin, an enzyme found in digestive and brain systems, thrombin, a coagulation cascade enzyme, and Lm-TL of a thrombin-like enzyme present in Lachesis muta venom that affects the prey central nervous system, among others, using bioinformatic tools. The analysis of the structural features of neuropsin and of these enzymes that present different and specific biological activities despite their high homology degree may help on designing selective inhibitor for treating several diseases including brain disorders.

Key words: Neuropsin, serine proteases, plasticity, homology, docking.