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Structural biology

Modelling collagen diseases

Nature volume 453, pages 998–999 (2008)Cite this article

Mutations in collagen lead to hereditary disorders such as brittle-bone disease. Peptide models for aberrant collagens are beginning to clarify how these amino-acid replacements lead to clinical problems.

Collagen is the predominant protein in the body defining the mechanical properties of tissues. In many hereditary connective-tissue disorders, collagen's regular repeating sequence of amino acids is disrupted. Short peptide chains have proved to be valuable models in understanding both these pathologies and normal collagens1. In the Journal of the American Chemical Society, Gauba and Hartgerink2 report an intriguing peptide model for osteogenesis imperfecta, a dominant hereditary disorder commonly known as brittle-bone disease. The model allowed them to make disease-related mutations in any or all of the three peptide chains that make up collagen.

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Figure 1: Collagen mutations mimicked by peptide models.

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Authors and Affiliations

  1. Barbara Brodsky is in the Department of Biochemistry, University of Medicine and Dentistry of New Jersey — Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA. brodsky@umdnj.edu,

    Barbara Brodsky

  2. Jean Baum is in the Department of Chemistry and Chemical Biology, BioMaPs Institute, Rutgers University, Piscataway, New Jersey 08854, USA. jean.baum@rutgers.edu,

    Jean Baum

Authors
  1. Barbara Brodsky
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  2. Jean Baum
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Brodsky, B., Baum, J. Modelling collagen diseases. Nature 453, 998–999 (2008). https://doi.org/10.1038/453998a

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