Cross-α/β polymorphism of PSMα3 fibrils

The formation of ordered cross-β amyloid protein aggregates is associated with a variety of human disorders. While conventional infrared methods serve as sensitive reporters of the presence of these amyloids, the recently discovered amyloid secondary structure of cross-α fibrils presents new questio...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2022-02, Vol.119 (5)
Main Authors: Cracchiolo, Olivia M, Edun, Dean N, Betti, Vincent M, Goldberg, Jacob M, Serrano, Arnaldo L
Format: Article
Language:English
Subjects:
Amyloid
Amyloid - genetics
Bacterial Toxins - genetics
Biofilms
Biological Sciences
Fibrillogenesis
Fourier transforms
Gene polymorphism
Infrared spectroscopy
Phenols
Physical Sciences
Polymorphism
Polymorphism, Genetic - genetics
Protein structure
Secondary structure
Spectrophotometry, Infrared - methods
Spectroscopy, Fourier Transform Infrared - methods
Spectrum analysis
Staphylococcus aureus - genetics
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Summary:The formation of ordered cross-β amyloid protein aggregates is associated with a variety of human disorders. While conventional infrared methods serve as sensitive reporters of the presence of these amyloids, the recently discovered amyloid secondary structure of cross-α fibrils presents new questions and challenges. Herein, we report results using Fourier transform infrared spectroscopy and two-dimensional infrared spectroscopy to monitor the aggregation of one such cross-α-forming peptide, phenol soluble modulin alpha 3 (PSMα3). Phenol soluble modulins (PSMs) are involved in the formation and stabilization of biofilms, making sensitive methods of detecting and characterizing these fibrils a pressing need. Our experimental data coupled with spectroscopic simulations reveals the simultaneous presence of cross-α and cross-β polymorphs within samples of PSMα3 fibrils. We also report a new spectroscopic feature indicative of cross-α fibrils.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.2114923119