Bioinformatic Analysis of Human Collagen Sequence Mutations on Osteogenesis Imperfecta

Abstract

Collagen has been implicated in a number of pathological conditions. When an amino acid in triple helix is replaced with other amino acids, the collagen structure is destroyed. The deterioration in the collagen structure causes various hereditary diseases and dysfunctions. In this study, the mutations on the alpha-1 chain of type I collagen, which is the most common in the human body, were examined using Python programming language. Based on the previous studies, brittle bone disease (OI) type 2 caused by mutations in type-I collagen alpha-1 chains, has been focused on. UniprotKB database were used for the mutations reported. The mutations obtained were combined in an alpha-I chain and it was seen that the most mutated amino acid was glycine (Gly). Since glycine amino acid affects the stability of the helix structure of the collagen alpha-I chain, it can be considered to influence collagen-induced diseases. The most frequently recurring mutations (glycine (G)> arginine (R), glycine (G)> serine (S), glycine (G)>aspartate (D)) were detected. As a result of comparison, increase in molecular mass, change in isoelectric point, decrease in hydropathy index, change in charge state and acid-base properties were observed. The effect of these changed features on brittle bone disease (OI) has been interpreted.