Journal
ACS CHEMICAL NEUROSCIENCE
Volume 10, Issue 8, Pages 3343-3345Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acschemneuro.9b00353
Keywords
Amyloidogenesis; amyloid beta; tip-enhanced Raman spectroscopy; toxic conversion; oligomers; protofibrils; fibrils
Funding
- UTEP
- UT STARS
- National Science Foundation (NSF) PREM program [DMR-1827745]
- NIH [1SC3 GM111200 01A1]
- NIH MBRS SCORE Border Biomedical Research Center at The University of Texas at El Paso
- Research Centers in Minority Institutions program of the National Institutes on Minority Health and Health Disparities, a component of the Research Center in Minority Institutions (RCMI) program [2G12MD007592, 5G12MD007592]
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Inroads into understanding the process by which amyloid proteins become toxic have been hampered by the lack of experimental techniques that adequately resolve the process. Recently, tip-enhanced Raman spectroscopy, with its unique capability to spectroscopically image and chemically identify reaction mixtures with nanoscale precision, was used to obtain a high-resolution roadmap of the soluble-to-toxic conversion of amyloid beta. This technique opens the door for studying the toxic aggregation pathways of other amyloid proteins and spurs efforts devoted to prophylactic and therapeutic intervention in neurodegenerative and protein-misfolding-related disorders.
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