Issue 32, 2015
From the journal:

Chemical Communications

Site-specific dynamics of amyloid formation and fibrillar configuration of Aβ1–23 using an unnatural amino acid†

Haiyang Liu,a   Richard Lantz,a   Patrick Cosme,a   Nelson Rivera,b   Carlos Andino,b   Walter G. Gonzalez,c   Andrew C. Terentis,a   Ewa P. Wojcikiewicz,d   Rolando Oyola,b   Jaroslava Miksovskac  and  Deguo Du*a  

* Corresponding authors

a Department of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL 33431, USA
E-mail: ddu@fau.edu

b Department of Chemistry, University of Puerto Rico-Humacao, Humacao, Puerto Rico 00791, Puerto Rico

c Department of Chemistry and Biochemistry, Florida International University, Miami, FL 33199, USA

d Department of Biomedical Science, Florida Atlantic University, Boca Raton, FL 33431, USA

Abstract

We identify distinct site-specific dynamics over the time course of Aβ1–23 amyloid formation by using an unnatural amino acid, p-cyanophenylalanine, as a sensitive fluorescent and Raman probe. Our results also suggest the key role of an edge-to-face aromatic interaction in the conformational conversion to form and stabilize β-sheet structure.

Graphical abstract: Site-specific dynamics of amyloid formation and fibrillar configuration of Aβ1–23 using an unnatural amino acid

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Article information

DOI
https://doi.org/10.1039/C5CC00149H
Article type
Communication
Submitted
07 Jan 2015
Accepted
18 Mar 2015
First published
18 Mar 2015

Chem. Commun., 2015,51, 7000-7003

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Site-specific dynamics of amyloid formation and fibrillar configuration of Aβ1–23 using an unnatural amino acid

H. Liu, R. Lantz, P. Cosme, N. Rivera, C. Andino, W. G. Gonzalez, A. C. Terentis, E. P. Wojcikiewicz, R. Oyola, J. Miksovska and D. Du, Chem. Commun., 2015, 51, 7000 DOI: 10.1039/C5CC00149H

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