Volume 135, Issue 51 e202314531
Forschungsartikel

Side-Chain Chemistry Governs Hierarchical Order of Charge-Complementary β-sheet Peptide Coassemblies

Dr. Renjie Liu

Dr. Renjie Liu

J. Crayton Pruitt Family Department of Biomedical Engineering, University of Florida, Gainesville, FL-32611 USA

These authors contributed equally to this work.

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Xin Dong

Xin Dong

Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC-27695 USA

These authors contributed equally to this work.

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Dr. Dillon T. Seroski

Dr. Dillon T. Seroski

J. Crayton Pruitt Family Department of Biomedical Engineering, University of Florida, Gainesville, FL-32611 USA

These authors contributed equally to this work.

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Dr. Bethsymarie Soto Morales

Dr. Bethsymarie Soto Morales

J. Crayton Pruitt Family Department of Biomedical Engineering, University of Florida, Gainesville, FL-32611 USA

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Dr. Kong M. Wong

Dr. Kong M. Wong

School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA-30332 USA

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Alicia S. Robang

Alicia S. Robang

School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA-30332 USA

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Lucas Melgar

Lucas Melgar

J. Crayton Pruitt Family Department of Biomedical Engineering, University of Florida, Gainesville, FL-32611 USA

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Prof. Thomas E. Angelini

Prof. Thomas E. Angelini

Department of Mechanical and Aerospace Engineering, University of Florida, Gainesville, FL-32611 USA

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Prof. Anant K. Paravastu

Prof. Anant K. Paravastu

School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA-30332 USA

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Prof. Carol K. Hall

Prof. Carol K. Hall

Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC-27695 USA

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Prof. Gregory A. Hudalla

Corresponding Author

Prof. Gregory A. Hudalla

J. Crayton Pruitt Family Department of Biomedical Engineering, University of Florida, Gainesville, FL-32611 USA

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First published: 06 November 2023

Abstract

Self-assembly of proteinaceous biomolecules into functional materials with ordered structures that span length scales is common in nature yet remains a challenge with designer peptides under ambient conditions. This report demonstrates how charged side-chain chemistry affects the hierarchical co-assembly of a family of charge-complementary β-sheet-forming peptide pairs known as CATCH(X+/Y−) at physiologic pH and ionic strength in water. In a concentration-dependent manner, the CATCH(6K+) (Ac-KQKFKFKFKQK-Am) and CATCH(6D−) (Ac-DQDFDFDFDQD-Am) pair formed either β-sheet-rich microspheres or β-sheet-rich gels with a micron-scale plate-like morphology, which were not observed with other CATCH(X+/Y−) pairs. This hierarchical order was disrupted by replacing D with E, which increased fibril twisting. Replacing K with R, or mutating the N- and C-terminal amino acids in CATCH(6K+) and CATCH(6D−) to Qs, increased observed co-assembly kinetics, which also disrupted hierarchical order. Due to the ambient assembly conditions, active CATCH(6K+)-green fluorescent protein fusions could be incorporated into the β-sheet plates and microspheres formed by the CATCH(6K+/6D−) pair, demonstrating the potential to endow functionality.

Conflict of interest

The authors declare no conflict of interest.

Data Availability Statement

The data that support the findings of this study are available from the corresponding author upon reasonable request.

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