In Silico Molecular Docking of HSPA2 with 4HNE in Human sperm

Abstract

Polyunsaturated fatty acids are susceptible to peroxidation and they yield various degradation products, including the main α,β-unsaturated hydroxyalkenal, 4-hydroxy-2,3-trans-nonenal (HNE) in oxidative stress. The molecule is highly reactive and able to react readily with various cellular components, such as DNA, proteins and other molecules containing nucleophilic thiol or amino groups. Protein-HNE adduct formation can lead to alterations in the normal functioning and modified activity of various proteins. HSPA2 is a testis-enriched member of the HSP70 family of chaperones, which is primarily responsible for preventing the aggregation of misfolded proteins and for fulfilling secondary roles in the transmembrane transport of client proteins and the formation of multimeric protein complexes. HSPA2 was present in the acrosomal domain of human spermatozoa as a major component of molecular complexes, in close association with just two other proteins, sperm adhesion molecule 1 (SPAM1) and arylsulfatase A (ARSA), both of which that have previously been implicated in sperm-egg interaction. HSPA2 is key target for 4HNE adduction reactions and that its chaperoning activity is particularly susceptible to such an insult. 4HNE adduction directly leads to a loss of HSPA2 chaperone activity and a subsequent perturbation of zona pellucida protein complex assembly. Aim: This study is to understand Which region of HSPA2 is bound to the 4HNE? Method: Cristal structure of human HSPA2 was ducked against 4HNE in a run by hex 8 and the interactions between them were analyzed in ligplus v.1.4.5 Results: The results showed that HSPA2/4HNE complex number of hydrogen bondages is 3 with binding energy -4.2. According to results 4HNE interact with HSPA2 but in a region other than our selective area.