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Self‐assembling amyloid‐like peptides as exogenous second harmonic probes for bioimaging applications
Author(s) -
Ni Ming,
Zhuo Shuangmu,
Iliescu Ciprian,
So Peter T. C.,
Mehta Jodhbir S.,
Yu Hanry,
Hauser Charlotte A. E.
Publication year - 2019
Publication title -
journal of biophotonics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.877
H-Index - 66
eISSN - 1864-0648
pISSN - 1864-063X
DOI - 10.1002/jbio.201900065
Subject(s) - amyloid (mycology) , amyloidosis , biophysics , peptide , chemistry , microscopy , nanotechnology , materials science , pathology , biochemistry , biology , medicine , inorganic chemistry
Amyloid‐like peptides are an ideal model for the mechanistic study of amyloidosis, which may lead to many human diseases, such as Alzheimer disease. This study reports a strong second harmonic generation (SHG) effect of amyloid‐like peptides, having a signal equivalent to or even higher than those of endogenous collagen fibers. Several amyloid‐like peptides (both synthetic and natural) were examined under SHG microscopy and shown they are SHG‐active. These peptides can also be observed inside cells (in vitro). This interesting property can make these amyloid‐like peptides second harmonic probes for bioimaging applications. Furthermore, SHG microscopy can provide a simple and label‐free approach to detect amyloidosis. Lattice corneal dystrophy was chosen as a model disease of amyloidosis. Morphological difference between normal and diseased human corneal biopsy samples can be easily recognized, proving that SHG can be a useful tool for disease diagnosis.