Analysis of Domains in Selected Plant and Animal Food Proteins - Precursors of Biologically Active Peptides - In Silico Approach

Abstract

In silico methods are useful tool in protein structure-functional relationships analysis. BIOPEP and InterPro databases were applied to analyze the presence of bioactive fragments in the domains occurring in the sequences representing the major groups of proteins. Domains found in the proteins analyzed had mostly transporting (bovine β-lactoglobulin), immunoglobulin-like (chicken connectin), alpha-amylase inhibitor (a/β-wheat gliadin), calcium binding (chicken myosin) functions, or allowed straightly to assign the protein to an appropriate superfamily (bovine casein). It confirmed the thesis about the existence of the functional relations between the structure (sequence) and the domains with identified conformation. Amongst the domains present in the protein sequences we revealed the presence of fragments with the activities: antihypertensive, opioid, dipeptidylpeptidase IV inhibitors, immunomodulating, and neuropeptides. In the chicken connectin within the immunoglobulin-like domain we found immunomodulating fragments. InterPro analysis did not reveal the existence of any domains in a soybean globulin. It can be explained by the lack of the key structure information helpful in the defining the structure-function relationships. As the number of information in the applied databases will continue to increase we can expect to find stronger relationships between bioactivity of fragments encrypted in proteins and the functionality of domains. This might allow in the future to find evolutionary similarity between different origin food proteins - sources of bioactive peptides.