Cu(II) Specifically Disassembles Insulin Amyloid Nanostructures via Direct Interaction with Cross-β Fibrils-Reference-Cited by-同舟云学术

Cu(II) Specifically Disassembles Insulin Amyloid Nanostructures via Direct Interaction with Cross-β Fibrils

Published:2024-07-11 Issue:32 Volume:24 Page:9784-9792
ISSN:1530-6984
Container-title:Nano Letters
language:en
Short-container-title:Nano Lett.

Author:

Mittal Shikha¹,Prajapati Kailash Prasad¹^ORCID,Ansari Masihuzzaman¹^ORCID,Joshi Kajal¹,Mishra Nishant²^ORCID,Mahato Om Prakash¹,Anand Bibin Gnanadhason²^ORCID,Kar Karunakar¹^ORCID

Affiliation:

1. Biophysical and Biomaterials Research Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India

2. Biomolecular Self-Assembly Lab, Department of Biotechnology, School of Bioengineering, SRM Institute of Science and Technology, Kattankulathur, Tamil Nadu 603203, India

Funder

Council of Scientific and Industrial Research, India

University Grants Commission

Science and Engineering Research Board

Department of Biotechnology, Ministry of Science and Technology, India

Department of Science and Technology, Ministry of Science and Technology, India

Jawaharlal Nehru University

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.nanolett.4c00113

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3. X-ray Absorption Spectroscopy Investigations of Copper(II) Coordination in the Human Amyloid β Peptide

4. Pulse EPR Spectroscopy Reveals the Coordination Sphere of Copper(II) Ions in the 1â16 Amyloid-Î² Peptide: A Key Role of the First Two N-Terminus Residues

5. Affinity of zinc and copper ions for insulin monomers