Designing Multifunctional Biomaterials via Protein Self-Assembly

Aleksei Solomonov, Anna Kozell, Ulyana Shimanovich*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

14 Citations (Scopus)

Abstract

Protein self-assembly is a fundamental biological process where proteins spontaneously organize into complex and functional structures without external direction. This process is crucial for the formation of various biological functionalities. However, when protein self-assembly fails, it can trigger the development of multiple disorders, thus making understanding this phenomenon extremely important. Up until recently, protein self-assembly has been solely linked either to biological function or malfunction; however, in the past decade or two it has also been found to hold promising potential as an alternative route for fabricating materials for biomedical applications. It is therefore necessary and timely to summarize the key aspects of protein self-assembly: how the protein structure and self-assembly conditions (chemical environments, kinetics, and the physicochemical characteristics of protein complexes) can be utilized to design biomaterials. This minireview focuses on the basic concepts of forming supramolecular structures, and the existing routes for modifications. We then compare the applicability of different approaches, including compartmentalization and self-assembly monitoring. Finally, based on the cutting-edge progress made during the last years, we summarize the current knowledge about tailoring a final function by introducing changes in self-assembly and link it to biomaterials' performance.This Minireview sums up cutting-edge concepts regarding the formation of protein-based supramolecular structures, compartmentalization, and self-assembly monitoring; it compares the routes of their modifications and applications in multifunctional biomaterial design. We summarize the current knowledge about machine learning/artificial intelligence applications for protein structure prediction/obtainment and link it to biomaterial performance.+image
Original languageEnglish
Article numbere202318365
Number of pages18
JournalAngewandte Chemie - International Edition
Volume63
Issue number14
DOIs
Publication statusPublished Online - 11 Jan 2024

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 authors would like to acknowledge partial support from the GMJ Schmidt Minerva Center of Supramolecular Architectures at the Weizmann Institute, Mondry Family Fund for University of Michigan/Weizmann collaboration, Gerald Schwartz and Heather Reisman Foundation, and 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, supported by a research grant from the Estate of David A. Fishstrom. The authors are also grateful to Steve Manch for editing the English in the manuscript.

All Science Journal Classification (ASJC) codes

  • Catalysis
  • General Chemistry

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