Effects of sound energy on proteins and their complexes

Anna Kozell, Aleksei Solomonov, Ulyana Shimanovich

Research output: Contribution to journalReview articlepeer-review

2 Scopus citations

Abstract

Mechanical energy in the form of ultrasound and protein complexes intuitively have been considered as two distinct unrelated topics. However, in the past few years, increasingly more attention has been paid to the ability of ultrasound to induce chemical modifications on protein molecules that further change protein–protein interaction and protein self-assembling behavior. Despite efforts to decipher the exact structure and the behavior-modifying effects of ultrasound on proteins, our current understanding of these aspects remains limited. The limitation arises from the complexity of both phenomena. Ultrasound produces multiple chemical, mechanical, and thermal effects in aqueous media. Proteins are dynamic molecules with diverse complexation mechanisms. This review provides an exhaustive analysis of the progress made in better understanding the role of ultrasound in protein complexation. It describes in detail how ultrasound affects an aqueous environment and the impact of each effect separately and when combined with the protein structure and fold, the protein–protein interaction, and finally the protein self-assembly. It specifically focuses on modifying role of ultrasound in amyloid self-assembly, where the latter is associated with multiple neurodegenerative disorders.

Original languageEnglish
Pages (from-to)3013-3037
Number of pages25
JournalFEBS Letters
Volume597
Issue number24
Early online date15 Oct 2023
DOIs
StatePublished - Dec 2023
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2023 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.

Funding

U.S. acknowledges financial support from the Nella and Leon Benoziyo Center for Neurological Diseases. In addition, U.S. thanks the Perlman family for funding the Shimanovich Lab at the Weizmann Institute of Science: ‘This research was made possible, in part, by the generosity of the Harold Perlman Family.’ The work was also supported by a research grant from the Perlman Family Foundation Founded by Anita and Louis Perlman C‐AIM Young Scientist Fund. The authors would like to acknowledge partial support from the GMJ Schmidt Minerva Center of Supramolecular Architectures at the Weizmann Institute, the Mondry Family Fund for the University of Michigan/Weizmann Collaboration, the Gerald Schwartz and Heather Reisman Foundation, and the WIS Sustainability and Energy Research Initiative (SAERI). This research was supported by a research grant from the Tom and Mary Beck Center for Advanced and Intelligent Materials at the Weizmann Institute of Science, Rehovot, Israel. Molecular graphics and analyses were performed with ucsf chimerax , developed by the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco, with support from the National Institutes of Health R01‐GM129325 and the Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases. The authors are also grateful to Steve Manch for the English editing.

FundersFunder number
Gerald Schwartz and Heather Reisman Foundation
Mondry Family Fund for the University of Michigan/Weizmann Collaboration
Perlman family for funding the Shimanovich Lab
SAERI
Tom and Mary Beck Center for Advanced and Intelligent Materials at the Weizmann Institute of Science, Rehovot, Israel
WIS Sustainability and Energy Research Initiative
Weizmann Institute
National Institutes of HealthR01‐GM129325
National Institute of Allergy and Infectious Diseases
Perlman Family Foundation
Weizmann Institute of Science

    Keywords

    • amyloid
    • cavitation
    • fibrillar protein self-assembly
    • ultrasound
    • β-sheet conformation

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