Metallopolymer−Peptide Conjugates: Synthesis and Self-Assembly of Polyferrocenylsilane Graft and Block Copolymers Containing a β-Sheet Forming Gly-Ala-Gly-Ala Tetrapeptide Segment
| Autor: | Ian Manners, Guido W. M. Vandermeulen, Zhuo Wang, Kyoung Taek Kim |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
chemistry.chemical_classification
Oligopeptide Polymers and Plastics Tetrapeptide Stereochemistry Molecular Conformation Temperature Bioengineering Peptide Silanes Antiparallel (biochemistry) Phenoxathiin Ring-opening polymerization Protein Structure Secondary Biomaterials End-group chemistry Materials Chemistry Self-assembly Oligopeptides |
| Zdroj: | Biomacromolecules. 7:1005-1010 |
| ISSN: | 1526-4602 1525-7797 |
| DOI: | 10.1021/bm050732p |
| Popis: | We describe the synthesis and self-assembly of two beta-sheet forming metallopolymer-peptide conjugates. The ability of the oligotetrapeptide sequence Gly-Ala-Gly-Ala (GAGA) to form antiparallel beta-sheets was retained in PFS-b-AGAG (PFS = polyferrocenylsilane) and PFS-g-AGAG conjugates with block and graft architectures, respectively. In the solid state, DSC experiments suggest a phase separation between the peptide and PFS domains. In toluene, PFS-b-AGAG interestingly forms a fibrous network which consists of a core containing the self-assembled antiparallel beta-sheet peptide and a corona of organometallic PFS. The self-assembly of the peptide into antiparallel beta-sheets is the driving force for the fiber formation, whereas PFS prevents uncontrolled lateral aggregation of the fibers. The use of an oligopeptide to self-assemble an otherwise random coiled organometallic polymer may be a useful strategy to enhance nanostructure formation. In the cases described here, the conjugates may be used to create nanopatterned ceramics, and the redox properties of the resulting supramolecular aggregates are of significant interest. |
| Databáze: | OpenAIRE |
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