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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，ＩｎＫｗ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ＩｎＫｗ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。
Prion proteins are a source of infection in chronic central nervous system degenerative diseases in humans and animals and sequences 113-120 of the protein are thought to play an important role in their pathogenicity and transmission mechanisms. Reversed-phase high performance liquid chromatography was used to analyze the chromatographic retention behavior of Prion protein 113-120. By comparing the chromatographic retention behaviors of the peptides under different mobile phases and different temperatures, it was found that the variation of InKw with temperature and the Van’t Hoff curve were relatively simple when using acetonitrile as the mobile phase, indicating that the polypeptide in acetonitrile solution In the conformation taken are more stable, less susceptible to temperature. When methanol solution is used as the mobile phase, the InKw of polypeptide with free end varies with temperature and the polypeptide whose Van’t Hoff curve is blocked by amide respectively than the terminal carboxyl and amino is complicated, indicating that the polypeptide with free end in methanol solution The conformation taken is relatively unstable and vulnerable to the environment. These results further prove that the 113-120 sequence may play an important role in the conformational changes of Prion protein.