Abstract
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.
Highlights
Peptide co-assembly is attractive for creating biomaterials with new forms and functions
A grand challenge in peptide coassembly is having the ability to accurately predict biomaterial structure and function from amino acid sequence information. These features are determined by peptide content of the nanofiber, which is difficult to ascertain in multicomponent systems due to the inability to distinguish self- and co-association events using conventional approaches
A difference in preference for self- versus co-association resulted in β-sheet nanofibers with disproportionate peptide content, and correlated with observed variances in morphology, features that cannot be presently predicted from primary sequence alone
Summary
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. A grand challenge in peptide coassembly is having the ability to accurately predict biomaterial structure and function from amino acid sequence information These features are determined by peptide content of the nanofiber, which is difficult to ascertain in multicomponent systems due to the inability to distinguish self- and co-association events using conventional approaches. The peptide component with the lower number of charged residues had greater propensity for strand mismatching (i.e., “self-association”) This observation may not be surprising, but when coupled with the limited sequence space that has been explored in peptide co-assembly, underscores the need for systematic studies to understand how molecular features influence nanofiber formation, composition, structure, and function
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