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Cu(II) Specifically Disassembles Insulin Amyloid Nanostructures via Direct Interaction with Cross-ß Fibrils.
Mittal, Shikha; Prajapati, Kailash Prasad; Ansari, Masihuzzaman; Joshi, Kajal; Mishra, Nishant; Mahato, Om Prakash; Anand, Bibin Gnanadhason; Kar, Karunakar.
Afiliación
  • Mittal S; Biophysical and Biomaterials Research Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India.
  • Prajapati KP; Biophysical and Biomaterials Research Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India.
  • Ansari M; Biophysical and Biomaterials Research Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India.
  • Joshi K; Biophysical and Biomaterials Research Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India.
  • Mishra N; Biomolecular Self-Assembly Lab, Department of Biotechnology, School of Bioengineering, SRM Institute of Science and Technology, Kattankulathur, Tamil Nadu 603203, India.
  • Mahato OP; Biophysical and Biomaterials Research Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India.
  • Anand BG; Biomolecular Self-Assembly Lab, Department of Biotechnology, School of Bioengineering, SRM Institute of Science and Technology, Kattankulathur, Tamil Nadu 603203, India.
  • Kar K; Biophysical and Biomaterials Research Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India.
Nano Lett ; 24(32): 9784-9792, 2024 Aug 14.
Article en En | MEDLINE | ID: mdl-38990555
ABSTRACT
In this work, we demonstrate direct evidence of the antiamyloid potential of Cu(II) ions against amyloid formation of insulin. The Cu(II) ions were found to efficiently disassemble the preformed amyloid nanostructures into soluble species and suppress monomer fibrillation under aggregation-prone conditions. The direct interaction of Cu(II) ions with the cross-ß structure of amyloid fibrils causes substantial disruption of both the interchain and intrachain interactions, predominantly the H-bonds and hydrophobic contacts. Further, the Cu(II) ions show a strong affinity for the aggregation-prone conformers of the protein and inhibit their spontaneous self-assembly. These results reveal the possible molecular mechanism for the antiamyloidogenic potential of Cu(II) which could be important for the development of metal-ion specific therapeutic strategies against amyloid linked complications.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cobre / Nanoestructuras / Amiloide / Insulina Límite: Humans Idioma: En Revista: Nano Lett Año: 2024 Tipo del documento: Article País de afiliación: India Pais de publicación: Estados Unidos
Texto completo
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Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cobre / Nanoestructuras / Amiloide / Insulina Límite: Humans Idioma: En Revista: Nano Lett Año: 2024 Tipo del documento: Article País de afiliación: India Pais de publicación: Estados Unidos