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

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

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, 200...

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Main Authors: Mohammed Inayathullah, Jayakumar Rajadas
Format: Article
Language:English
Published: Elsevier 2016-06-01
Series:Data in Brief
Online Access:http://www.sciencedirect.com/science/article/pii/S2352340916302840
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spelling doaj-604f669ed05d48a6a5dc26a3bb6981432020-11-25T01:41:56ZengElsevierData in Brief2352-34092016-06-01716431651Effect of osmolytes on the conformation and aggregation of some amyloid peptides: CD spectroscopic dataMohammed Inayathullah0Jayakumar Rajadas1Biomaterials and Advanced Drug Delivery Laboratory, School of Medicine, Stanford University, Palo Alto, CA 94304, USA; Bioorganic and Neurochemistry Laboratory, Central Leather Research Institute, Adyar, Chennai, Tamilnadu 600020, India; Cardiovascular Pharmacology Division, Cardiovascular Institute, School of Medicine, Stanford University, Stanford, CA 94305, USABiomaterials and Advanced Drug Delivery Laboratory, School of Medicine, Stanford University, Palo Alto, CA 94304, USA; Cardiovascular Pharmacology Division, Cardiovascular Institute, School of Medicine, Stanford University, Stanford, CA 94305, USA; Correspondence to: Stanford University 1050 Arastradero Road, Room A148, Palo Alto, CA 94304, USA. Tel.: 650 724 6806; fax: 650 721 4651.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) [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) [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 (http://dx.doi.org/10.2174/0929867023369187) (Gazit, 2002) [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. Keywords: Amyloid β-protein, Aggregation, Circular dichroism, Conformation, Islet amyloid polypeptide, Osmolytes, Peptides, Polyglutaminehttp://www.sciencedirect.com/science/article/pii/S2352340916302840
collection DOAJ
language English
format Article
sources DOAJ
author Mohammed Inayathullah
Jayakumar Rajadas
spellingShingle Mohammed Inayathullah
Jayakumar Rajadas
Effect of osmolytes on the conformation and aggregation of some amyloid peptides: CD spectroscopic data
Data in Brief
author_facet Mohammed Inayathullah
Jayakumar Rajadas
author_sort Mohammed Inayathullah
title Effect of osmolytes on the conformation and aggregation of some amyloid peptides: CD spectroscopic data
title_short Effect of osmolytes on the conformation and aggregation of some amyloid peptides: CD spectroscopic data
title_full Effect of osmolytes on the conformation and aggregation of some amyloid peptides: CD spectroscopic data
title_fullStr Effect of osmolytes on the conformation and aggregation of some amyloid peptides: CD spectroscopic data
title_full_unstemmed Effect of osmolytes on the conformation and aggregation of some amyloid peptides: CD spectroscopic data
title_sort effect of osmolytes on the conformation and aggregation of some amyloid peptides: cd spectroscopic data
publisher Elsevier
series Data in Brief
issn 2352-3409
publishDate 2016-06-01
description 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) [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) [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 (http://dx.doi.org/10.2174/0929867023369187) (Gazit, 2002) [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. Keywords: Amyloid β-protein, Aggregation, Circular dichroism, Conformation, Islet amyloid polypeptide, Osmolytes, Peptides, Polyglutamine
url http://www.sciencedirect.com/science/article/pii/S2352340916302840
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