Narcissistic Self-Sorting of Amphiphilic Collagen-Inspired Peptides in Supramolecular Vesicular Assembly
Herein, we describe the hierarchical self-assembly accompanying self-sorting of collagen-inspired peptides (CPs). The two amphiphilic CPs used in this study contained an azobenzene (Az) moiety at the N-terminal, connected through a flexible spacer, but with different lengths of the (Gly-Pro-Hyp)n tr...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 38(2022), 7 vom: 22. Feb., Seite 2294-2300 |
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| Weitere Verfasser: | , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2022
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Peptides Collagen 9007-34-5 |
| Zusammenfassung: | Herein, we describe the hierarchical self-assembly accompanying self-sorting of collagen-inspired peptides (CPs). The two amphiphilic CPs used in this study contained an azobenzene (Az) moiety at the N-terminal, connected through a flexible spacer, but with different lengths of the (Gly-Pro-Hyp)n triplet (n = 5 and 7). When the CP aqueous solution (60 °C) was cooled to 4 °C, both CPs formed a triple helix structure and the pre-organized helices subsequently self-assembled into highly ordered vesicles with a diameter of 50-200 nm. Interestingly, narcissistic self-sorting was observed in both triple helix- and matured vesicle-formation processes, when the two CPs were mixed. Owing to the difference in the propensity for triple helix formation with temperature, the two CPs discriminate each other in response to a temperature change and form two kinds of triple helix foldamers, each containing a single component. The resulting differences in the amphiphilic balance and molecular length between the foldamers appear to allow individual self-sorting to form distinct vesicles. Furthermore, such vesicular assemblies were found to disassemble upon UV irradiation via trans-cis isomerization of the Az-groups. These findings offer important insights into the design of new complex but ordered, peptide self-assembly systems with potential applications in nanobiotechnology |
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| Beschreibung: | Date Completed 08.03.2022 Date Revised 08.03.2022 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.1c02978 |