Nanoscale Structure of Poly(Ethylene Glycol) Hybrid Block Copolymers containing Amphiphilic β-Strand Peptide Sequences
| Autor: | Valeria Castelletto, Ian W. Hamley, Harm-Anton Klok, Annette Rösler, Oleksandr O. Mykhaylyk |
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| Rok vydání: | 2003 |
| Předmět: |
Nanostructure
Polymers and Plastics Polymers Molecular Sequence Data Bioengineering Peptide Crystallography X-Ray Antiparallel (biochemistry) Protein Structure Secondary Polyethylene Glycols Biomaterials chemistry.chemical_compound Spectroscopy Fourier Transform Infrared Amphiphile Polymer chemistry Materials Chemistry Copolymer Nanotechnology Amino Acid Sequence chemistry.chemical_classification Polymer Crystallography chemistry Attenuated total reflection Peptides Ethylene glycol |
| Zdroj: | Biomacromolecules. 4:859-863 |
| ISSN: | 1526-4602 1525-7797 |
| DOI: | 10.1021/bm034058s |
| Popis: | This paper discusses the solid state and melt nanoscale structure of a series of novel poly(ethylene glycol) (PEG) hybrid di- and triblock copolymers, which contain amphiphilic beta-strand peptide sequences. The block copolymers have been prepared via solid-phase synthesis, affording perfectly monodisperse peptide segments with a precisely defined alpha-amino acid sequence. Attenuated total reflection Fourier transform infrared spectroscopy and X-ray scattering experiments indicate that the self-assembly properties of the peptide sequences are retained upon conjugation to PEG and mediate the formation of an ordered superstructure consisting of alternating PEG layers and peptide domains with an highly organized antiparallel beta-sheet structure. The results suggest that combination of biological structural motifs with synthetic polymers may be a versatile strategy for the development of novel self-assembled materials with complex internal structures and the potential to interface with biology. |
| Databáze: | OpenAIRE |
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