Controlling Amphiphilic Polymer Folding beyond the Primary Structure with Protein-Mimetic Di(Phenylalanine)
| Autor: | Peter A. Dykeman-Bermingham, Abigail S. Knight, Jacqueline L. Warren |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
chemistry.chemical_classification
Circular dichroism Chemistry Polymers Phenylalanine Molecular Conformation General Chemistry Biochemistry Catalysis Article Protein mimetic Hydrophobic effect Folding (chemistry) chemistry.chemical_compound Surface-Active Agents Colloid and Surface Chemistry Monomer Polymer chemistry Copolymer Non-covalent interactions Protein secondary structure |
| Zdroj: | J Am Chem Soc |
| ISSN: | 1520-5126 |
| Popis: | While methods for polymer synthesis have proliferated, their functionality pales in comparison to natural biopolymers – strategies are limited for building the intricate network of noncovalent interactions necessary to elicit complex, protein-like functions. Using a bioinspired di(phenylalanine) acrylamide (FF) monomer, we explored the impact of various non-covalent interactions in generating ordered assembled structures. Amphiphilic copolymers were synthesized that exhibit β-sheet-like local structure upon collapsing into single-chain assemblies in aqueous environments. Systematic analysis of a series of amphiphilic copolymers illustrated that the global collapse is primarily driven by hydrophobic forces. Hydrogen-bonding and aromatic interactions stabilize local structure, as β-sheet-like interactions were identified via circular dichroism and thioflavin T fluorescence. Similar analysis of phenylalanine (F) and alanine-phenylalanine acrylamide (AF) copolymers found that distancing the aromatic residue from the polymer backbone is sufficient to induce β-sheet-like local structure akin to the FF copolymers; however, the interactions between AF subunits are less stable than those formed by FF. Further, hydrogen-bond donating hydrophilic monomers disrupt internal structure formed by FF within collapsed assemblies. Collectively, these results illuminate design principles for the facile incorporation of multiple facets of protein-mimetic, higher-order structure within folded synthetic polymers. |
| Databáze: | OpenAIRE |
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