Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: A review

Dmitry Kurouski; Richard P. Van Duyne; Igor K. Lednev

doi:10.1039/c5an00342c

Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: A review

Dmitry Kurouski^*, Richard P. Van Duyne, Igor K. Lednev

^*Corresponding author for this work

Research output: Contribution to journal › Review article › peer-review

162 Scopus citations

Abstract

Amyloid fibrils are β-sheet rich protein aggregates that are strongly associated with various neurodegenerative diseases. Raman spectroscopy has been broadly utilized to investigate protein aggregation and amyloid fibril formation and has been shown to be capable of revealing changes in secondary and tertiary structures at all stages of fibrillation. When coupled with atomic force (AFM) and scanning electron (SEM) microscopies, Raman spectroscopy becomes a powerful spectroscopic approach that can investigate the structural organization of amyloid fibril polymorphs. In this review, we discuss the applications of Raman spectroscopy, a unique, label-free and non-destructive technique for the structural characterization of amyloidogenic proteins, prefibrilar oligomers, and mature fibrils.

Original language	English (US)
Pages (from-to)	4967-4980
Number of pages	14
Journal	Analyst
Volume	140
Issue number	15
DOIs	https://doi.org/10.1039/c5an00342c
State	Published - Feb 5 2015

ASJC Scopus subject areas

Analytical Chemistry
Biochemistry
Environmental Chemistry
Spectroscopy
Electrochemistry

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title = "Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: A review",

abstract = "Amyloid fibrils are β-sheet rich protein aggregates that are strongly associated with various neurodegenerative diseases. Raman spectroscopy has been broadly utilized to investigate protein aggregation and amyloid fibril formation and has been shown to be capable of revealing changes in secondary and tertiary structures at all stages of fibrillation. When coupled with atomic force (AFM) and scanning electron (SEM) microscopies, Raman spectroscopy becomes a powerful spectroscopic approach that can investigate the structural organization of amyloid fibril polymorphs. In this review, we discuss the applications of Raman spectroscopy, a unique, label-free and non-destructive technique for the structural characterization of amyloidogenic proteins, prefibrilar oligomers, and mature fibrils.",

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AU - Kurouski, Dmitry

AU - Van Duyne, Richard P.

AU - Lednev, Igor K.

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N2 - Amyloid fibrils are β-sheet rich protein aggregates that are strongly associated with various neurodegenerative diseases. Raman spectroscopy has been broadly utilized to investigate protein aggregation and amyloid fibril formation and has been shown to be capable of revealing changes in secondary and tertiary structures at all stages of fibrillation. When coupled with atomic force (AFM) and scanning electron (SEM) microscopies, Raman spectroscopy becomes a powerful spectroscopic approach that can investigate the structural organization of amyloid fibril polymorphs. In this review, we discuss the applications of Raman spectroscopy, a unique, label-free and non-destructive technique for the structural characterization of amyloidogenic proteins, prefibrilar oligomers, and mature fibrils.

AB - Amyloid fibrils are β-sheet rich protein aggregates that are strongly associated with various neurodegenerative diseases. Raman spectroscopy has been broadly utilized to investigate protein aggregation and amyloid fibril formation and has been shown to be capable of revealing changes in secondary and tertiary structures at all stages of fibrillation. When coupled with atomic force (AFM) and scanning electron (SEM) microscopies, Raman spectroscopy becomes a powerful spectroscopic approach that can investigate the structural organization of amyloid fibril polymorphs. In this review, we discuss the applications of Raman spectroscopy, a unique, label-free and non-destructive technique for the structural characterization of amyloidogenic proteins, prefibrilar oligomers, and mature fibrils.

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Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: A review

Abstract

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