激光生物学报摘要, 更新时间: 2007年10月13日
  由美国生科集团 (BVTech, Inc.) 主办
  
XeCI准分子紫外激光辐照生物大分子BSA(Ⅴ)对其蛋白质结构的影响
激光生物学报摘要 2007-4

黄汝多,查向栋,李振华,朱 峰,陈 涛,智小勇,陈永荣,殷宝龙,胡能书 (1. 安徽大学生命科学院,安徽 合肥230039;2.中国科学院安徽光学精密机械研究所, 安徽 合肥230031; 3.湖南师范大学生命科学学院,湖南 长沙410081)

摘 要:XeCI(380 nm)准分子紫外激光(单脉冲输出能量25 mJ,33.3 mJ~34.4 mJ脉冲频率每秒两次,光斑15 mm×7 mm或4.5 mm×0.5 mm,透镜焦距300 mm),辐照小牛血清白蛋白「BSA(Ⅴ)」固体或液体样品的时间分别为15 s,30 s,45 s,和60 s;样品距激光光源的距离分别为:150 mm,250 mm,290 mm,340 mm。改变激光参量辐照小牛血清白蛋白样品和其对照,用光谱法测试其FT-IR(IR),Vis-UV(UV),FR光谱,并比较分析。受辐照后的BSA(Ⅴ)与主链构象相关的酰胺平面的特征FT-IR谱线,特别是与蛋白质二级结构敏感的酰胺面Ⅰ,1652 cm-1;与 α-螺旋结构相关的FT-IR 1140 cm-1~500 cm-1;及与蛋白质侧链氨基酸残基Tyr,Phe,Trp相关的特征峰UV 277.6 nm ,UV 216 nm和FR 340 nm,FR 680 nm 的峰强度(T % 或 OF %或Q %)和它们的峰位(cm-1或nm)均受激光辐照的影响,其影响程度与使用的XeCI激光参量的改变有一定的敏感性和相关性。实验结果与讨论对认识激光生物学效应的分子机理,探索建立激光-生物学效应的关系参数,以便进一步发现新的有效的激光生物学效应,发现和认识潜在(后继)的 正负面的激光生物学效应,进而加以调控有一定的理论与实用参考价值。


The Effect of XeCl Excimer Laser Radiation on Biomacromolecule Structure BSA(Ⅴ)

HUANG Ruo-duo1, ZHA Xiang-dong1, LI Zhen-hua1, ZHU Feng1, CHEN Tao1, ZHI Xiao yong1, CHEN Yong-rong2, YIN Bao-long2, HU Neng -shu3 (1. School of Life Science, Anhui University, Hefei 230039, Anhui, China; 2. Anhui institute of Optics and Fine Mechanics, Chinese Academy of Science, Hefei 230031, Anhui,China;3.School of Life Science, Hunan Normal University, Changsha 410081,Hunan,China)

Abstract: The biomacromolecule of bovine serum albumin fractionⅤpowder or it's solution was radiated separately by XeCl excimer laser(308nm)in the condition of export out power 25mJ/per pulse or 33.3~34.4 mJ/per pulse, pulse frequency 2 times/s. The radiation samples were set on difference distance:150 mm,250mm,290mm,or 340mm. Far from laser source, and went through different radiation time:15s,30s,45s or 60s. The radiated samples of BSA(Ⅴ) and their control were measured by FT-IR, Vis-UV, and FR, then they were observed and analyzed, and compared with the above two data, The results showed that;realative BSAⅤSample protein structure(confomation)spectra, which is either protein main-chain FT-IR spectra lines(peaks),special for theamide plate-Ⅰ,1 652cm-1,or the protein side-chain amino acid residuce groups, Tyr, Phe, Trp, spectra lines 277.6 nm,216 nm(UV),340 nm,680 nm(FR),their peak intensity and the peak position all appeared great changers, and the changing degree of the radiating samples spectra is corresponding to the changing of the radiation parameters on the samples. It shows that laser is an important environmental factor to the cause the structure(comformation change)of protein in the microconic structure area, and make bio-signal transfer.


 

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