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Adv. Mater., Feb 09 2025, | https://doi.org/10.1002/adma.202419941
Harnessing Amino Acid Modularity for Programmable Function in Covalent Peptide Assemblies
Yun-Mi Hur 1,2, Kyoung-Ik Min 1,2,3
1Department of Biomedical Convergence Science and Technology, Kyungpook National University, Daegu, 41566, Republic of Korea.
2Cell and Matrix Research Institute, Kyungpook National University, Daegu, 41944, Republic of Korea.
3Department of Advanced Bioconvergence, Kyungpook National University, Daegu, 41566, Republic of Korea.
Corresponding Author: Kyoung-Ik Min
1Department of Biomedical Convergence Science and Technology, Kyungpook National University, Daegu, 41566, Republic of Korea.
2Cell and Matrix Research Institute, Kyungpook National University, Daegu, 41944, Republic of Korea.
3Department of Advanced Bioconvergence, Kyungpook National University, Daegu, 41566, Republic of Korea.
Corresponding Author: Kyoung-Ik Min
Abstract
Covalent peptide assembly leverages robust covalent bonds and dynamic non-covalent interactions to provide enhanced stability and introduce diverse functionalities. Nevertheless, it remains significantly challenging to achieve modular control over the structural diversity and functional complexity while elucidating how specific amino acid sequences contribute to these processes. Here, the systematic encoding of peptide derivative characteristics is demonstrated through amino acid modularity to enable precise control over both the structural diversity and functional complexity in covalent peptide assemblies. By systematically screening single amino acid substitutions in pentapeptides using tyrosine crosslinking, a diverse library of peptide constructs is developed. Each construct is tailored to exhibit distinct properties, including charge repulsion, aggregation-induced quenching, disassembly behavior, and redox responsiveness. The strategic manipulation of sequence composition, both in individual assemblies and combinatorial systems, enables programmable control over the structural diversity and functional complexity. This approach yields various module-specific functions, including frustrated growth, hierarchical hollow architecture formation, affinity enrichment, stimuli-responsive behavior, and fluorescence signal amplification. This work establishes a framework for the design of modular peptide materials with programmable functionalities, advancing the development of next-generation multicomponent peptide assembly technologies characterized by unprecedented complexity and adaptability.
논문정보
- Research article
- 2025년 02월 (BRIC 등록일 2025-02-17)
- 국내 연구진
- 바이오·의료융합 > 바이오센싱 및 나노바이오물질
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