Análise estrutural e funcional in silico de uma PR-5 do tipo osmotina de Physalis angulata com potencial atividade farmacológico.

Abstract

Computational or in silico analyzes mimic biological information for deduced proteins from its gene sequences. These analyzes have been widely used in Medicinal Chemistry for the rational design of new drugs assisted by computer and represent powerful tools to investigate the structure and function of biomolecules and their complexes, when there are available experimental protein structures generated by crystallography or magnetic resonance which share high similarity with the amino acid sequences of interest. Due to its importance as antimicrobial protein of interest to biotechnological applications, the aim of this study was to perform the comparative structural and functional analysis of a Physalis angulata osmotinlike PR-5 protein, from its gene sequence, using bioinformatics strategies. The Swissmodel program was used to construct a three-dimensional model for PaOLP through molecular modeling by homology. The model was validated by analysis of ANOLEA, QMEAN6, GROMOS, Ramachandran and ProSe in relation to the energy and location of amino acid residues. The proposed model for PaOLP was considered stable and presented very close representation of the real structure of the protein. The structure of the PaOLP active site presented typical functional features for the family of osmotin-like PR-5 proteins. PaOLP bind strongly to the adiponectin receptor whose interaction was proven by electrostatic energy, in which three residues of PaOLP were the hotspot of the interaction. PaOLP shared high amino acids sequence similarity with the tobacco osmotin, proven agonist to adiponectin receptor, possessing functional residues conserved between them. Hence, PaOLP is a good target to be explored as an alternative agonist to adiponectin receptor, which is available and free of intellectual property.