Charge guides pathway selection in β-sheet fibrillizing peptide co-assembly

Dillon T. Seroski, Xin Dong, Kong M. Wong, Renjie Liu, Qing Shao, Anant K. Paravastu, Carol K. Hall, Gregory A. Hudalla

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


Peptide co-assembly is attractive for creating biomaterials with new forms and functions. Emergence of these properties depends on the peptide content of the final assembled structure, which is difficult to predict in multicomponent systems. Here using experiments and simulations we show that charge governs content by affecting propensity for self- and co-association in binary CATCH(+/−) peptide systems. Equimolar mixtures of CATCH(2+/2−), CATCH(4+/4−), and CATCH(6+/6−) formed two-component β-sheets. Solid-state NMR suggested the cationic peptide predominated in the final assemblies. The cationic-to-anionic peptide ratio decreased with increasing charge. CATCH(2+) formed β-sheets when alone, whereas the other peptides remained unassembled. Fibrillization rate increased with peptide charge. The zwitterionic CATCH parent peptide, “Q11”, assembled slowly and only at decreased simulation temperature. These results demonstrate that increasing charge draws complementary peptides together faster, favoring co-assembly, while like-charged molecules repel. We foresee these insights enabling development of co-assembled peptide biomaterials with defined content and predictable properties.

Original languageEnglish
Article number172
JournalCommunications Chemistry
Issue number1
StatePublished - Dec 2020

Bibliographical note

Funding Information:
This research was supported by the National Science Foundation (RAISE 1743432). We would also like to thank Dr. Michael Harris (Dept. of Chemistry, University of Florida) for access and time on his CD spectrophotometer.

Publisher Copyright:
© 2020, The Author(s).

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry (all)
  • Environmental Chemistry
  • Materials Chemistry


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