Research Highlights

One fatal error

doi:10.1038/nindia.2009.250 Published online 21 July 2009

Researchers have found the genetic mutation responsible for the substitution of an amino acid in collagen-like peptides1. This increases the risk of a disease similar to brittle bone disease. The insight is important for the designing of peptides with new biological activity and protein engineering.

Mutations in genes may replace amino acids leading to structural defect in proteins and peptides resulting in diseases. The researchers chose a collagen-like peptide and launched computer-based models through molecular dynamics (MD) method to explore the outcome of amino acid substitution.

The substitution of an amino acid created large local disruption to the triple-helical structure. Analysis of MD yielded a bulge at the site of substitution affecting overall stability of the model collagen-like peptide. The researchers calculated the energy needed for each alanine (amino acid) substitution, which was similar to the value for the glycine to alanine mutation in collagen.

Since the glycine to alanine mutation is involved in genetic disorders such as osteogenesis imperfecta (OI, a type of brittle bone disease), such change may produce a similar effect on collagen.

The authors of this work are from: Chemical Laboratory, Central Leather Research Institute, CSIR, Adyar, Chennai and Department of Science and Technology, New Delhi, India.


  1. Punitha, V. et al. Molecular Dynamics Investigations on the Effect of d Amino Acid Substitution in a Triple-Helix Structure and the Stability of Collagen. J. Phys. Chem. B. 113, 8983-8992 (2009) | Article |