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50Hz脉冲电场作用下胰岛素构象变化的拉曼光谱分析 被引量:6

Raman Analysis of Conformation Changes of Insulin Solvent after Being Exposed to ELF Pulsed Electric Field
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摘要 以激光拉曼光谱为手段,研究了经50Hz脉冲电场作用后,胰岛素分子构象的变化。分析表明经50Hz低频脉冲电场作用后,胰岛素分子的共价键体系仍保持完好,但是分子的氢键体系发生了改变。主要表现在α螺旋结构遭到破坏,α螺旋相对于β折叠的含量降低,致使酰胺Ⅰ带的峰向高波数方向移动。α螺旋结构的解聚使原本位于螺旋内部的振动暴露。三个二硫键的强度均减弱,且向短波方向稍有移动,也说明其周围的微环境发生了变化。另外,胰岛素二聚体之间的氢键遭破坏,导致相关拉曼峰的出现或者增强。 Raman spectra of insulin solvents are presented before and after being exposed to the pulsed electric field with extremely low frequency 50 Hz(ELF). The covalences of the molecule were not affected and the changes of some secondary bonds such as hydrogen bonds and salt bonds were observed. Detailed analysis of these spectra indicates that the a-helix of insulin molecule was destroyed after the exposure, which is proved by the shift of the peak of the amide I region toward higher wave number and by the appearance of several new peakss: 1 561 and 1 594 cm(-1). Uhe disulfides were affected by the weaken a-helix, and their vibrational moees were changed. Meanwhile the hydrogen bonding between the dimer are broken down which leads to the increase in the peak intensities at 1 002 and at 1 602 cm(-1).
出处 《光谱学与光谱分析》 SCIE EI CAS CSCD 北大核心 2004年第11期1331-1333,共3页 Spectroscopy and Spectral Analysis
基金 国家自然科学基金(50137030) 上海市科技发展基金(022312114)资助项目
关键词 胰岛素 作用 改变 暴露 微环境 含量 Α螺旋 构象变化 Β折叠 低频脉冲电场 insulin solvent 50 Hz pulsed electric field Raman conformation changes
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参考文献5

  • 1[2]Brandenburg Dietrich, Wollmer Axel. Insulin Chemistry, Structure and Function of Insulin and Related Hormones, in Proceeding of Second International Insulin Symposium Aachen Germany, 1980.
  • 2[3]Reipa V, Gsigalas A, Abramowitz S. J. Electroanal. Chem., 1993, 348: 413.
  • 3[6]Yu Nai-Teng, Liu C S. J. Mol. Biol., 1972, 70: 117.
  • 4[7]Venyaminov S Yu, Kalnin N N. Biopolymers, 1990, 30(13-14): 1243.
  • 5[8]Isaish pittman I V. Biochemistry, 1995, 34: 10578.

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