波谱学杂志 ›› 2015, Vol. 32 ›› Issue (2): 283-290.doi: 10.11938/cjmr20150211

• 研究论文 • 上一篇    下一篇

人类唾液蛋白N 端片段的构型

郭玹铭1,张七凤2,陈振中1*   

  1. 1. 台湾大学 化学系,台湾 台北 106;2. 基因体研究中心,台湾 台北 115
  • 收稿日期:2015-02-11 修回日期:2015-05-13 出版日期:2015-06-05 发布日期:2015-06-05
  • 作者简介:*通讯联系人:陈振中,电话:+886-2-33662994, E-mail: chanjcc@ntu.edu.tw.
  • 基金资助:


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.
  • Supported by:


摘要:

人类唾液蛋白Statherin 是含有43 残基的酸性磷酸化蛋白.此蛋白对磷酸钙具有较高的吸附性,已知其N 端15 残基的片段(SN-15)会吸附于磷灰石的表面.在该工作中,作者以液体核磁共振波谱学研究SN-15 的分子结构.圆二色光谱显示SN-15 在磷酸盐缓冲溶液中具α 螺旋构型.根据高分辨核磁共振氢谱(COSY,TOCSY 及NOESY)作者得到相关的NOE 及J 耦合数据,氢氘交换实验也进一步显示SN-15 具α 螺旋构型.

关键词: 生物成矿, 磷灰石, SN-15

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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