Hybrid Conjugates Formed between Gold Nanoparticles and an Amyloidogenic Diphenylalanine‐Cysteine Peptide. Issue 24 (25th June 2018)
- Record Type:
- Journal Article
- Title:
- Hybrid Conjugates Formed between Gold Nanoparticles and an Amyloidogenic Diphenylalanine‐Cysteine Peptide. Issue 24 (25th June 2018)
- Main Title:
- Hybrid Conjugates Formed between Gold Nanoparticles and an Amyloidogenic Diphenylalanine‐Cysteine Peptide
- Authors:
- Pelin, Juliane N. B. D.
Gatto, Emanuela
Venanzi, Mariano
Cavalieri, Francesca
Oliveira, Cristiano L. P.
Martinho, Herculano
Silva, Emerson R.
Aguilar, Andrea M.
Souza, Juliana S.
Alves, Wendel A. - Abstract:
- Abstract: We investigated the effect of gold nanoparticles (AuNPs) on the aggregation of a CFF (C=cysteine; F=phenylalanine) tripeptide (derived from A β peptide) in aqueous medium. Special attention was dedicated to the role of AuNPs as inducers and inhibitors during nucleation kinetics and the structure of the resulting scaffolds was carefully investigated. At millimolar concentrations, the tripeptide was found to form β ‐sheet structures organized into long filaments. Spectral signatures and topography of the filaments were studied by Raman spectroscopy and atomic force microscopy (AFM), revealing that conjugation to AuNPs not only stabilizes the system, but also inhibit or enhance amyloid‐like features depending on the synthesis route used in the preparation of AuNPs. Sodium borohydride (NaBH4 ) mediated synthesis of AuNPs gave rise to a strong absorption peak close to 520 nm, indicating that AuNPs were dispersed, independently of the peptide concentration added in the reaction. However, when the peptide/gold salt mixture was heated at 60 °C, AuNPs and AuNP‐decorated filaments were both formed in solution and the fractions of which population were found to be dependent on the [HAuCl4 ]/[CFF] ratio, as illustrated by TEM images. In addition, the insertion of AuNPs at the surface of CFF nanostructures can promote electron transfer from the metallic nanoparticles to the CFF surface, creating an n ‐type semiconductor, and causing a peak shift of the phenylalanine absorptionAbstract: We investigated the effect of gold nanoparticles (AuNPs) on the aggregation of a CFF (C=cysteine; F=phenylalanine) tripeptide (derived from A β peptide) in aqueous medium. Special attention was dedicated to the role of AuNPs as inducers and inhibitors during nucleation kinetics and the structure of the resulting scaffolds was carefully investigated. At millimolar concentrations, the tripeptide was found to form β ‐sheet structures organized into long filaments. Spectral signatures and topography of the filaments were studied by Raman spectroscopy and atomic force microscopy (AFM), revealing that conjugation to AuNPs not only stabilizes the system, but also inhibit or enhance amyloid‐like features depending on the synthesis route used in the preparation of AuNPs. Sodium borohydride (NaBH4 ) mediated synthesis of AuNPs gave rise to a strong absorption peak close to 520 nm, indicating that AuNPs were dispersed, independently of the peptide concentration added in the reaction. However, when the peptide/gold salt mixture was heated at 60 °C, AuNPs and AuNP‐decorated filaments were both formed in solution and the fractions of which population were found to be dependent on the [HAuCl4 ]/[CFF] ratio, as illustrated by TEM images. In addition, the insertion of AuNPs at the surface of CFF nanostructures can promote electron transfer from the metallic nanoparticles to the CFF surface, creating an n ‐type semiconductor, and causing a peak shift of the phenylalanine absorption band. Abstract : We show that the gold nanoparticles may both affect the structure of a short amyloid‐like peptide in aqueous medium and promote electron transfer from the metallic nanoparticles to the peptide surface, creating an n ‐type semiconductor. … (more)
- Is Part Of:
- ChemistrySelect. Volume 3:Issue 24(2018)
- Journal:
- ChemistrySelect
- Issue:
- Volume 3:Issue 24(2018)
- Issue Display:
- Volume 3, Issue 24 (2018)
- Year:
- 2018
- Volume:
- 3
- Issue:
- 24
- Issue Sort Value:
- 2018-0003-0024-0000
- Page Start:
- 6756
- Page End:
- 6765
- Publication Date:
- 2018-06-25
- Subjects:
- Amyloids -- Crystal nucleation and growth -- Gold nanoparticles -- n-type semiconductor -- Peptide assemblies
Chemistry -- Periodicals
540.5 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)2365-6549 ↗ - DOI:
- 10.1002/slct.201801345 ↗
- Languages:
- English
- ISSNs:
- 2365-6549
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3172.241000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 6872.xml