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dc.contributor.authorAlghrably, Mawadda
dc.contributor.authorCzaban, Iwona
dc.contributor.authorJaremko, Lukasz
dc.contributor.authorJaremko, Mariusz
dc.date.accessioned2018-11-13T06:49:06Z
dc.date.available2018-11-13T06:49:06Z
dc.date.issued2018-11-10
dc.identifier.citationAlghrably M, Jaremko Ł, Czaban I, Jaremko M (2018) Interaction of amylin species with transition metals and membranes. Journal of Inorganic Biochemistry. Available: http://dx.doi.org/10.1016/j.jinorgbio.2018.11.004.
dc.identifier.issn0162-0134
dc.identifier.doi10.1016/j.jinorgbio.2018.11.004
dc.identifier.urihttp://hdl.handle.net/10754/629864
dc.description.abstractIslet Amyloid Polypeptide (IAPP), also known as amylin, is a 37-amino-acid peptide hormone that is secreted by pancreatic islet β-cells. Amylin is complementary to insulin in regulating and maintaining blood glucose levels in the human body. The misfolding and aggregation of amylin is primarily associated with type 2 diabetes mellitus, which is classified as an amyloid disease. Recently, the interactions between amylin and specific metal ions, e.g., copper(II), zinc(II), and iron(II), were found to impact its performance and aggregation processes. Therefore, the focus in this review will be on how the chemistry and structural properties of amylin are affected by these interactions. In addition, the impact of amylin and other amyloidogenic peptides interacting with metal ions on the cell membranes is discussed. In particular, recent studies on the interactions of amylin with copper, zinc, iron, nickel, gold, ruthenium, and vanadium are discussed.
dc.description.sponsorshipAuthors would like to thank King Abdullah University of Science and Technology (KAUST) for financial support.
dc.publisherElsevier BV
dc.relation.urlhttps://www.sciencedirect.com/science/article/pii/S0162013418304409
dc.rightsNOTICE: this is the author’s version of a work that was accepted for publication in Journal of Inorganic Biochemistry. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Inorganic Biochemistry, [, , (2018-11-10)] DOI: 10.1016/j.jinorgbio.2018.11.004 . © 2018. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectDiabetes type II
dc.subjectTransition metals
dc.subjectAmylin
dc.subjectAggregation
dc.subjectAggregation inhibition
dc.subjectComplex formation
dc.titleInteraction of amylin species with transition metals and membranes
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.identifier.journalJournal of Inorganic Biochemistry
dc.eprint.versionPost-print
kaust.personAlghrably, Mawadda
kaust.personJaremko, Lukasz
kaust.personCzaban, Iwona
kaust.personJaremko, Mariusz
refterms.dateFOA2018-11-13T07:09:28Z
dc.date.published-online2018-11-10
dc.date.published-print2019-02


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