Chinese Journal of Magnetic Resonance ›› 2015, Vol. 32 ›› Issue (2): 283-290.doi: 10.11938/cjmr20150211

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Conformation of the N-Terminal Fragment of Human Salivary Statherin

GUO Syuan-ming1,CHANG Chi-fon2,CHAN Jerry C C1*   

  1. 1. Department of Chemistry, Taiwan University, Taipei 106, China; 2. Genomics Research Center, Taipei 115, China

  • Received:2015-02-11 Revised:2015-05-13 Online:2015-06-05 Published:2015-06-05
  • About author:*Corresponding author: CHAN Jerry C C, Tel: +886-2-33662994, E-mail: chanjcc@ntu.edu.tw.
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Abstract:

Human salivary statherin is a 43-residue acidic phosphoprotein present in human saliva, possessing a high affinity for calcium phosphate minerals such as hydroxyapatite. The N-terminal 15-residue fragment of statherin (SN-15) is known to bind strongly to the crystallites of hydroxyapatite. In this work, we investigate the conformation of SN-15 in aqueous solution by NMR. Analysis of the CD spectra shows that SN-15 adopts an α-helical structure in phosphate buffer. High-resolution proton NMR spectra (COSY, TOCSY, and NOESY) have been acquired, from which the NOE patterns and J-couplings of amide hydrogens have been obtained. Together with the constraints obtained from amide-hydrogen exchange experiments, the molecular structure of SN-15 has shown to be a continuous α-helical structure.

Key words: biomineralization, HAp, SN-15

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