Relationship Between Retention Behavior And Conformational Stability Of Reversed-Phase Liquid Chromatography Of Prion Protein 113-120 Sequence Polypeptides
Keywords
Prion Protein, Reversed-Phase High Performance Liquid Chromatography, Chromatographic Retention Behavior, Peptide Conformation
Abstract
Prion protein is the source of infection for chronic central nervous system degenerative diseases in humans and animals. The 113-120 sequence of the protein is considered to play an important role in its pathogenesis and infection mechanism. Reversed-phase high-performance liquid chromatography was used as the Analytical methods were used to study the chromatographic retention behavior of the Prion protein 113-120 sequence polypeptide. By comparing the changes in the chromatographic retention behavior of the polypeptide under different temperatures and different mobile phase conditions, it was found that when acetonitrile solution was used as the mobile phase, lnKw changed with temperature. The relationship and Van’tHoff curve are relatively simple, indicating that the conformation adopted by the polypeptide in acetonitrile solution is relatively stable and not easily affected by temperature. When methanol solution is used as the mobile phase, the lnKw of the polypeptide with free ends changes with temperature. and Van’tHoff curves are more complex than those of polypeptides whose terminal carboxyl and amino groups are blocked by amides respectively, indicating that the conformation adopted by polypeptides with free terminals in methanol solution is relatively unstable and susceptible to environmental influences. These results further prove that 113 The -120 sequence may play an important role in the conformational changes of Prion protein.
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Original research done by Guo Minliang,Milton,T.,W.,Hearn,Balvant,Sitaram
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