| Affiliation: | 1. Department of Chemistry, Collage of Chemistry and Chemical Engineering, Xiamen University, The MOE Key Laboratory of Spectrochemical Analysis and Instrumentation, Xiamen, 361005 China;2. State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, National Institute of Diagnostics and Vaccine Development in Infectious Disease, School of Life Sciences, School of Public Health, Xiamen University, Xiamen, 361102 China;3. Department of Chemical Physicals, University of Science and Technology of China, Hefei, 230026 China;4. X-ray Science Division, Argonne National Laboratory, Lemont, IL 60439 USA;5. Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, 310024 China;6. Department of Chemistry, Collage of Chemistry and Chemical Engineering, Xiamen University, The MOE Key Laboratory of Spectrochemical Analysis and Instrumentation, Xiamen, 361005 China Innovation Laboratory for Sciences and Technologies of Energy Materials of Fujian Province (IKKEM), Xiamen, 361005 China;7. Department of Chemistry, Emory University, Atlanta, GA 30033 USA |
| Abstract: | Advanced applications of biomacromolecular assemblies require a stringent degree of control over molecular arrangement, which is a challenge to current synthetic methods. Here we used a neighbor-controlled patterning strategy to build multicomponent peptide fibrils with an unprecedented capacity to manipulate local composition and peptide positions. Eight peptides were designed to have regulable nearest neighbors upon co-assembly, which, by simulation, afforded 412 different patterns within fibrils, with varied compositions and/or peptide positions. The fibrils with six prescribed patterns were experimentally constructed with high accuracy. The controlled patterning also applies to functionalities appended to the peptides, as exemplified by arranging carbohydrate ligands at nanoscale precision for protein recognition. This study offers a route to molecular editing of inner structures of peptide assemblies, prefiguring the uniqueness and richness of patterning-based material design. |
