Biomaterials

TREEting Rheumatoid Arthritis

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Science  20 May 2011:
Vol. 332, Issue 6032, pp. 896-897
DOI: 10.1126/science.332.6032.896-d

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  • Hydrogen bond donors and acceptors in collagens and rheumatoid arthritis
    • Qiuyun Liu, Professor, Guangdong Provincial Key Laboratory of Improved Variety Reproduction in Aquatic Economic Animals, Sun Yat-sen University
    • Other Contributors:
      • Shaoping Weng, Professor, Guangdong Provincial Key Laboratory of Improved Variety Reproduction in Aquatic Economic Animals, Sun Yat-sen University
      • Baojian Li, Professor, School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, China
      • Xiaoyi Hu, Researcher, Department of Medicine, Division of Immunology, Columbia University Medical Center, New York 10032, USA
      • Yunfan Shi, Student, School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, China
      • Wenliang Zhou, Professor, School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, China

    Collagen is the most abundant protein in mammals as the major constituent of connective tissues (1). Proline and hydroxyproline constitute about 20% of collagens. Hydroxyprolines were derived from prolines by the hydroxylation of prolines on propeptide. The hydrogen bonding capacity of these amino acid residues may underlie certain human diseases, such as rheumatoid arthritis that is induced by wet and cold conditions. In high humidity situation, the nitrogen atom and the carboxyl oxygen of proline and hydroxyproline as well as the hydroxyl oxygen of the latter can generate hydrogen bonds with protons and water; while in cold condition, the Krebs cycle and other pathways of energy metabolism produce protons which can form hydrogen bonds with proline and hydroxyproline. Collagen induced arthritis in animal models in a previous report (2). Furthermore, contributions from other hydrogen bond donors and acceptors exacerbate the effects brought about by the high content of proline and hydroxyproline. The carbon chemical shielding shown by the σ22 element for the deprotonated carboxyl groups supports the presence of strong hydrogen bonds with the carbonyl oxygen of certain amino acids (3). The σ22 element for the deprotonated carboxyl group in glycine corroborates the existence of moderate strength hydrogen bonds with the carbonyl oxygen (3). However the long bond length of carbonyl carbon with carbonyl oxygen in glycine (3) suggests that carbonyl oxygen in glycine may be strong...

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    Competing Interests: None declared.

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