Effect of osmolytes on the conformation and aggregation of some amyloid peptides: CD spectroscopic data

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• 作者：Mohammed Inayathullah^a ; ^b ; ^c ; Jayakumar Rajadas^a ; ^c ; ^{jayraja@stanford.edu" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Amyloid β-protein ; Aggregation ; Circular dichroism ; Conformation ; Islet amyloid polypeptide ; Osmolytes ; Peptides ; Polyglutamine
• 刊名：Data in Brief
• 出版年：2016
• 出版时间：June 2016
• 年：2016
• 卷：7
• 期：Complete
• 页码：1643-1651
• 全文大小：2638 K

文摘

Protein misfolding and aggregation are responsible for a large number of diseases called protein conformational diseases or disorders that include Alzheimer׳s disease, Huntington׳s diseases, Prion related encephalopathies and type-II diabetes (http://dx.doi.org/10.1038/35041139) (Kopito and Ron, 2000) ib1">[1]. A variety of studies have shown that some small organic molecules, known as osmolytes have the ability to stabilize native conformation of proteins and prevent misfolding and aggregation (http://www.la-press.com/article.php?article_id=447) (Zhao et al., 2008) ib2">[2]. It has been shown that certain short segment or fragment of respective proteins can also form amyloids, and the segments also promote the aggregation in the full-length protein (23369187">http://dx.doi.org/10.2174/0929867023369187) (Gazit, 2002) ib3">[3]. This article presents circular dichroism spectroscopic data on conformational analysis and effect of osmolytes on Aβ peptide fragments, different lengths of polyglutamine peptide and the amyloidogenic segment of islet amyloid polypeptide.