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

Autor: Liu, Renjie, Dong, Xin, Seroski, Dillon T., Soto Morales, Bethsymarie, Wong, Kong M., Robang, Alicia S., Melgar, Lucas, Angelini, Thomas E., Paravastu, Anant K., Hall, Carol K., Hudalla, Gregory A.
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Zdroj: Angewandte Chemie International Edition; 12/18/2023, Vol. 62 Issue 51, p1-13, 13p
Abstrakt: 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. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index