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

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 convers...

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Veröffentlicht in:	Chemical communications (Cambridge, England) England), 2015-04, Vol.51 (32), p.7000-7003
Hauptverfasser:	Liu, Haiyang, Lantz, Richard, Cosme, Patrick, Rivera, Nelson, Andino, Carlos, Gonzalez, Walter G, Terentis, Andrew C, Wojcikiewicz, Ewa P, Oyola, Rolando, Miksovska, Jaroslava, Du, Deguo
Format:	Artikel
Sprache:	eng
Schlagworte:	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
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Beschreibung
Zusammenfassung:	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.
ISSN:	1364-548X
DOI:	10.1039/c5cc00149h