Cystine oligomers successfully attached to peptide cysteine-rich fibrils

doi:10.1007/s11705-016-1554-6

Front. Chem. Sci. Eng.

2016, Vol. 10

Issue (1) : 99-102 https://doi.org/10.1007/s11705-016-1554-6

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Cystine oligomers successfully attached to peptide cysteine-rich fibrils

Christian Bortolini,Mingdong Dong(

)

Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus C 8000, Denmark

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Abstract

Amyloid peptides are renowned to be related to neurodegenerative diseases, however, a fruitful avenue is to employ them as high-performance nanomaterials. These materials benefit from the intrinsic outstanding mechanical robustness of the amyloid backbone made of b-strands. In this work, we exploited amyloid-like fibrils as functional material to attach pristine L-cysteine aggregates (cystine oligomers) and gold nanoparticles, without the need of templating compounds. This work will open new avenues on functional materials design and their realisation.

Keywords cysteine peptide fibrils gold nanoparticles amyloids oligomers nanomaterials

Corresponding Author(s): Mingdong Dong

Online First Date: 25 January 2016 Issue Date: 29 February 2016

Cite this article:

Christian Bortolini,Mingdong Dong. Cystine oligomers successfully attached to peptide cysteine-rich fibrils[J]. Front. Chem. Sci. Eng., 2016, 10(1): 99-102.

URL:

https://academic.hep.com.cn/fcse/EN/10.1007/s11705-016-1554-6
https://academic.hep.com.cn/fcse/EN/Y2016/V10/I1/99

Fig.1 Schematic of the monomer and compounds employed in this work. (a) Molecular representation of the peptide monomer NH₂-CSSFAFASSC-NH₂; the functional amino acid, i.e., cysteine, is highlighted in red; (b) Suggested scenario where pristine L-cysteines in solution bind each other forming cystine aggregates

Fig.2 Negative stained TEM images showing (a) amyloid-like twisted CSFAC fibrils, (b) pristine L-cysteine aggregates (cystine oligomers), and (c) CSFAC fibrils decorated with cystine oligomers

Fig.3 Negative stained TEM images presenting (a) cystine oligomers+ Au NPs, (b) detailed image showing Au NPs binding the cystine oligomers, and (c) CSFAC fibrils decorated with cystine oligomers and Au NPs

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