分析化学
分析化學
분석화학
CHINESE JOURNAL OF ANALYTICAL CHEMISTRY
2001年
6期
633-636
,共4页
郭敏亮%Balvant Sitaram%Guo Minliang%Milton T.WHearn
郭敏亮%Balvant Sitaram%Guo Minliang%Milton T.WHearn
곽민량%Balvant Sitaram%Guo Minliang%Milton T.WHearn
朊病毒蛋白%反相高效液相色谱%色谱保留行为%多肽构象
朊病毒蛋白%反相高效液相色譜%色譜保留行為%多肽構象
원병독단백%반상고효액상색보%색보보류행위%다태구상
朊病毒(Prion)蛋白是人和动物慢性中枢神经系统退化病的传染源,该蛋白的113-120序列被认为在其致病和传染机理中起着重要作用。以反相高效液相色谱为分析手段,研究了Prion蛋白113-120序列多肽的色谱保留行为。通过比较不同温度、不同流动相条件下该多肽色谱保留行为的变化,发现在以乙腈溶液为流动相时,lnKw随温度的变化关系和Van′t Hoff 曲线均比较简单,说明该多肽在乙腈溶液中所采取的构象均较稳定,不易受温度的影响。以甲醇溶液为流动相时,具有游离末端的多肽的lnKw随温度变化关系和Van′t Hoff曲线比末端羧基和氨基分别被酰胺封闭的多肽要复杂,说明具有游离末端的多肽在甲醇溶液中所采取的构象相对较不稳定,易受环境的影响。这些结果进一步证明,113-120序列在Prion蛋白构象变化中可能起着重要作用。
朊病毒(Prion)蛋白是人和動物慢性中樞神經繫統退化病的傳染源,該蛋白的113-120序列被認為在其緻病和傳染機理中起著重要作用。以反相高效液相色譜為分析手段,研究瞭Prion蛋白113-120序列多肽的色譜保留行為。通過比較不同溫度、不同流動相條件下該多肽色譜保留行為的變化,髮現在以乙腈溶液為流動相時,lnKw隨溫度的變化關繫和Van′t Hoff 麯線均比較簡單,說明該多肽在乙腈溶液中所採取的構象均較穩定,不易受溫度的影響。以甲醇溶液為流動相時,具有遊離末耑的多肽的lnKw隨溫度變化關繫和Van′t Hoff麯線比末耑羧基和氨基分彆被酰胺封閉的多肽要複雜,說明具有遊離末耑的多肽在甲醇溶液中所採取的構象相對較不穩定,易受環境的影響。這些結果進一步證明,113-120序列在Prion蛋白構象變化中可能起著重要作用。
원병독(Prion)단백시인화동물만성중추신경계통퇴화병적전염원,해단백적113-120서렬피인위재기치병화전염궤리중기착중요작용。이반상고효액상색보위분석수단,연구료Prion단백113-120서렬다태적색보보류행위。통과비교불동온도、불동류동상조건하해다태색보보류행위적변화,발현재이을정용액위류동상시,lnKw수온도적변화관계화Van′t Hoff 곡선균비교간단,설명해다태재을정용액중소채취적구상균교은정,불역수온도적영향。이갑순용액위류동상시,구유유리말단적다태적lnKw수온도변화관계화Van′t Hoff곡선비말단최기화안기분별피선알봉폐적다태요복잡,설명구유유리말단적다태재갑순용액중소채취적구상상대교불은정,역수배경적영향。저사결과진일보증명,113-120서렬재Prion단백구상변화중가능기착중요작용。
Prions are the infectious agents of the transmissible spongiform encephalopathies. The sequence 113-120 of Prion proteins is thought to be the most highly amyloidogenic peptide. The chromatographic retention behaviors of Prion 113-120 peptide on C18-column were studied under reversed-phase high-performance liquid chromatographic conditions with isocratic elution. When aquo-acetonitrile mobile phases were used, the temperature-depending relationships of lnkw and Van′t Hoff plots of both peptides with free termini and with capped termini were simple. The results demonstrated that the conformations adopted by both peptides in aquo-acetonitrile mobile phases were relatively stable, and could not be perturbed by temperature. When aquo-methanol mobile phases were used, the temperature-depending relationships of lnkw and Van′t Hoff plots of peptide with free termini were more complicated than that of peptide with capped termini. These results demonstrated that the conformations adopted by peptide with free termini in aquo-methanol mobile phases were relatively unstable and could be perturbed by circumstance. All these results further demonstrate that the sequence 113-120 could play an important role in the conformational change of Prion proteins.