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Nanomaterials 2019, 9(3), 412; https://doi.org/10.3390/nano9030412

Chiral Effect at Nano-Bio Interface: A Model of Chiral Gold Nanoparticle on Amylin Fibrillation

1,†
,
1,†
,
2,†
,
1
,
1
and
1,*
1
State Key Laboratory of Advanced Technology for Materials Synthesis and Processing, Wuhan University of Technology, No.122 Luoshi Road, Wuhan 430070, China
2
School of Arts and Media, Wuhan Vocational College of Software and Engineering, No. 117 Guanggu Road, Wuhan 430205, China
*
Author to whom correspondence should be addressed.
These authors contributed equally.
Received: 2 February 2019 / Revised: 25 February 2019 / Accepted: 5 March 2019 / Published: 11 March 2019
(This article belongs to the Special Issue Synthesis and Applications of Functionalized Gold Nanosystems)
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Abstract

Protein/Peptide amyloidosis is the main cause of several diseases, such as neurodegenerative diseases. It has been widely acknowledged that the unnatural fibrillation of protein/peptides in vivo is significantly affected by the physical and chemical properties of multiscale biological membranes. For example, previous studies have proved that molecule chirality could greatly influence the misfolding, fibrillation and assembly of β-Amyloid peptides at the flat liquid-solid surface. However, how the nanoscale chirality influences this process remains unclear. Here we used gold nanoparticles (AuNPs, d = 4 ± 1 nm)—modified with N-isobutyl-L(D)-cysteine (L(D)-NIBC) enantiomers—as a model to illustrate the chiral effect on the amylin fibrillation at nano-bio interface. We reported that both two chiral AuNPs could inhibit amylin fibrillation in a dosage-dependent manner but the inhibitory effect of L-NIBC-AuNPs was more effective than that of D-NIBC-AuNPs. In-situ real time circular dichroism (CD) spectra showed that L-NIBC-AuNPs could inhibit the conformation transition process of amylin from random coils to α-helix, while D-NIBC-AuNPs could only delay but not prevent the formation of α-helix; however, they could inhibit the further conformation transition process of amylin from α-helix to β-sheet. These results not only provide interesting insight for reconsidering the mechanism of peptides amyloidosis at the chiral interfaces provided by biological nanostructures in vivo but also would help us design therapeutic inhibitors for anti-amyloidosis targeting diverse neurodegenerative diseases. View Full-Text
Keywords: chiral AuNPs; nano-bio interface; amylin; fibrillation chiral AuNPs; nano-bio interface; amylin; fibrillation
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Li, J.; Chen, R.; Zhang, S.; Ma, Z.; Luo, Z.; Gao, G. Chiral Effect at Nano-Bio Interface: A Model of Chiral Gold Nanoparticle on Amylin Fibrillation. Nanomaterials 2019, 9, 412.

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