Barcoding Amino Acids for Mutation Screening in Amyloid Beta Peptides
Type
ArticleAuthors
HOANG, PHUONG
Khashab, Niveen M.

KAUST Department
Advanced Membranes and Porous Materials Research CenterChemical Engineering Program
Chemical Science Program
Physical Science and Engineering (PSE) Division
Smart Hybrid Materials (SHMs) lab
Date
2019-10-03Permanent link to this record
http://hdl.handle.net/10754/658657
Metadata
Show full item recordAbstract
Amino acid (AA) substitutions are directly correlated with specific pathologies such as Alzheimer's disease, making their rapid screening and detection critical to treatment and scientific study. A proof-of-concept implementation of the label-free and noninvasive Raman spectroscopy technique for the detection of AA substitutions in primary peptide fragments is demonstrated. By encoding the Raman “fingerprint” of individual AAs into binary formats called optical identification tags (OITs), a library of identifiers is created, which can then be used for detecting mutations. When the recorded Raman signal is enhanced by using surface-enhanced Raman scattering substrate, the mutation screening strategy can detect a single point missense mutation in an 11-AA peptide fragment of amyloid beta Aβ(25–35) and a frameshift mutation in a 42-AA fragment Aβ(1–42) down to picomolar concentrations. The combination of high sensitivity and simple operation makes the use of OITs a promising approach for high-throughput automated screening.Citation
Hoang, P., & Khashab, N. M. (2019). Barcoding Amino Acids for Mutation Screening in Amyloid Beta Peptides. Small Methods, 1900611. doi:10.1002/smtd.201900611Sponsors
This work was supported by King Abdullah University of Science and Technology (KAUST). The authors gratefully acknowledge useful conversations with Dr. Emily Ringe. The authors also acknowledge Dr. Jeremy A. Bau for proofreading the manuscript. They also thank Ivan Gromicho, a scientific illustrator at KAUST, for creating Figure 1 and ToC image.Publisher
WileyJournal
Small MethodsAdditional Links
https://onlinelibrary.wiley.com/doi/abs/10.1002/smtd.201900611ae974a485f413a2113503eed53cd6c53
10.1002/smtd.201900611