LiQiang CHEN, ChengZhi HUANG, ShuJun ZHEN, PingPing HU
{"title":"多肽与朊蛋白相互作用研究","authors":"LiQiang CHEN, ChengZhi HUANG, ShuJun ZHEN, PingPing HU","doi":"10.1360/zb2010-40-6-733","DOIUrl":"https://doi.org/10.1360/zb2010-40-6-733","url":null,"abstract":"Prion diseases are a class of central nervous system degenerative diseases involving a variety of animal and human beings. Presently, prion diseases have taken place in many countries in the world, which possess a great threat to human health. However, there is no effective treatment against these diseases. Previous investigations showed that the sequence-related peptides play an important role in stabilizing the conformation of prion protein. We performed a biochemical study of the 180I point mutation (a valine to isoleucine mutation) in this communication. As this mutation is near the glycosylation site at position 181, it plays an important role in the pathological prion disease. In this report, we designed four <italic>αxyzβ</italic> type peptides for sequence range of 182-190 of 180I. The results showed that only the sequence of EVVKK can bring a very good stability, and induce the conformation changes from <italic>β</italic>-sheet to <italic>α</italic>-helix, while the effect of other three peptides can be neglected, which can act as a reference for the development of peptide drugs, and further for the clinical treatment.","PeriodicalId":515091,"journal":{"name":"SCIENTIA SINICA Chimica","volume":"40 6","pages":"733-738"},"PeriodicalIF":0.0,"publicationDate":"2010-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147909276","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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