Site-specific dynamics of amyloid formation and fibrillar configuration of Aβ(1-23) using an unnatural amino acid

Haiyang Liu; Richard Lantz; Patrick Cosme; Nelson Rivera; Carlos Andino; Walter G Gonzalez; Andrew C Terentis; Ewa P Wojcikiewicz; Rolando Oyola; Jaroslava Miksovska; Deguo Du

doi:10.1039/c5cc00149h

Site-specific dynamics of amyloid formation and fibrillar configuration of Aβ(1-23) using an unnatural amino acid

Chem Commun (Camb). 2015 Apr 25;51(32):7000-3. doi: 10.1039/c5cc00149h. Epub 2015 Mar 24.

Authors

Haiyang Liu¹, Richard Lantz, Patrick Cosme, Nelson Rivera, Carlos Andino, Walter G Gonzalez, Andrew C Terentis, Ewa P Wojcikiewicz, Rolando Oyola, Jaroslava Miksovska, Deguo Du

Affiliation

¹ Department of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL 33431, USA. ddu@fau.edu.

PMID: 25801393
DOI: 10.1039/c5cc00149h

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Alanine / analogs & derivatives*
Alanine / chemistry
Amino Acid Sequence
Amyloid beta-Peptides / chemistry*
Amyloid beta-Peptides / metabolism
Models, Molecular
Molecular Sequence Data
Nitriles / chemistry*
Protein Structure, Secondary

Substances

Amyloid beta-Peptides
Nitriles
p-cyanophenylalanine
Alanine