Journal
COMMUNICATIONS CHEMISTRY
Volume 3, Issue 1, Pages -Publisher
NATURE RESEARCH
DOI: 10.1038/s42004-020-00414-w
Keywords
-
Categories
Funding
- National Science Foundation [RAISE 1743432]
Ask authors/readers for more resources
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 beta -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 beta -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. Co-assembly of peptide mixtures can yield interesting materials, but predictive understanding of assembly pathways is lacking. Here the self- and co-assembly preferences of oppositely-charged peptides are systematically studied experimentally and by molecular dynamics simulations.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available