The role of copper(ii) in the aggregation of human amylin-Reference-Cited by-同舟云学术

The role of copper(ii) in the aggregation of human amylin

Published:2014 Issue:10 Volume:6 Page:1841-1852
ISSN:1756-5901
Container-title:Metallomics
language:en
Short-container-title:Metallomics

Author:

Sinopoli Alessandro¹²³,Magrì Antonio⁴⁵³,Milardi Danilo⁴⁵³,Pappalardo Matteo⁶²³,Pucci Pietro⁶⁷⁸,Flagiello Angela⁶⁷⁸,Titman Jeremy J.⁹¹⁰¹¹¹²,Nicoletti Vincenzo Giuseppe¹³²³¹⁴¹⁵,Caruso Giuseppe¹⁶³,Pappalardo Giuseppe⁴⁵³,Grasso Giuseppe⁶²³

Affiliation:

1. Dottorato Internazionale in Biomedicina Traslazionale

2. Università degli Studi di Catania

3. Catania, Italy

4. Istituto Biostrutture e Bioimmagini

5. CNR

6. Dipartimento di Scienze Chimiche

7. Università degli Studi di Napoli Federico II

8. Napoli, Italy

9. School of Chemistry

10. University of Nottingham

11. University Park

12. Nottingham NG7 2RD, UK

13. Dipartimento di Scienze Biomediche (Sezione di Biochimica)

14. Istituto Nazionale di Biostrutture e Biosistemi (INBB) - sez. Biomolecole

15. Consorzio Interuniversitario

16. Dottorato Internazionale in Neurobiologia, Università degli Studi di Catania

Abstract

Copper(ii) coordination to human amylin has an influence on the aggregation and cytotoxic features of the polypeptide. Comparative investigations, carried out on a model peptide encompassing the 17–29 aminoacid region of amylin containing the putative metal binding site, support the non-fibrillar nature of the copper(ii) complexes.

Publisher

Oxford University Press (OUP)

Subject

Metals and Alloys,Biochemistry,Biomaterials,Biophysics,Chemistry (miscellaneous)

Link

http://pubs.rsc.org/en/content/articlepdf/2014/MT/C4MT00130C

Reference47 articles.

1. -Amyloid Monomers Are Neuroprotective

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3. Amylin

4. Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology

5. Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus

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