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 journalReview articlepeer-review

115 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 languageEnglish (US)
Pages (from-to)4967-4980
Number of pages14
JournalAnalyst
Volume140
Issue number15
DOIs
StatePublished - Feb 5 2015

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Environmental Chemistry
  • Spectroscopy
  • Electrochemistry

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