In silico assessment of self-assembly and bioactivity profiles of peptides from Lentil Proteins

In silico assessment of self-assembly and bioactivity profiles of peptides from Lentil Proteins

Matthew D. Ezema,1,2 Toluwase H. Fatoki2. Seyi Ogunrinola1, Chibuike C. Udenigwe1

1School of Nutrition Sciences, Faculty of Health sciences, University of Ottawa, Ottawa, ON K1H 8M5, Canada

2Department of Biochemistry, Federal University Oye-Ekiti, Ekiti State, Nigeria

Abstract

Peptides are usually less than 40 amino acids, ubiquitously generated during proteolytic cleavage or maturation of functional proteins. Peptides serve diverse biological functions and some can assemble spontaneously into a variety of nanostructures (nanoparticles, nanosheets, nanofibers, and nanotubes), thereby finding applications in a wide variety of fields, such as bioadhesives, hydrogels, and drug delivery systems. The aim of this study was to computationally assess the self-assembly and bioactivity profiles of lentil peptides obtained by mass spectrometry analyses from our previous work. The computational methods used involved prediction of peptide self-aggregation, bioactivity, physicochemical properties, three-dimensional structure and molecular dynamics. The result of self-aggregation potential of the lentil peptides from our database of 1146 peptides showed that only 44 peptides were amyloid-like at the energy threshold of -5.00 PASTA energy unit (PEU), which is equivalent to 5.960 kcal.mol-1. Moreover, only seven peptides: peptide 1137 (YVIVNDSCYHQLVSHWLNT), peptide 711 (LVVVPQNF), peptide 1143 (YVVVNDSCYHQL), peptide 493 (IVFWMYNDQDTPVIA), peptide 571 (LDIFVNSVE), peptide 494 (IVHIAKQL), and peptide 1062 (WMYNDQDTPVIAV) were predicted to be non-toxic. Overall, this study identified peptide 1137 (YVIVNDSCYHQLVSHWLNT) as the best candidate for further development, based on its moderate self-assembly profile, non-toxicity, moderate bioactivity, physicochemical properties, high 3D structure sOPEP energy and moderate molecular dynamics properties.

Keywords: Lentil peptides, self-assembly, amyloid formation, bioactivity, 3D structure, molecular dynamics.