Molecular Architecture Influences the Thermally Induced Aggregation Behavior of Elastin-like Polypeptides
| Autor: | Ali Ghoorchian, Nolan B. Holland |
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| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular chemistry.chemical_classification Protein Folding Quantitative Biology::Biomolecules Polymers and Plastics Protein Stability Transition temperature Bioengineering Polymer Recombinant Proteins Elastin Biomaterials chemistry.chemical_compound chemistry Nephelometry and Turbidimetry Materials Chemistry Biophysics Transition Temperature Amino Acid Sequence Elastin like polypeptides Protein Multimerization Peptides Protein Structure Quaternary Algorithms |
| Zdroj: | Biomacromolecules. 12:4022-4029 |
| ISSN: | 1526-4602 1525-7797 |
| DOI: | 10.1021/bm201031m |
| Popis: | Elastin-like polypeptides are thermally responsive polymers that exhibit phase separation above a transition temperature. The effect of molecular architecture on the temperature responsive behavior of elastin-like polypeptide solutions was investigated by characterization of solutions of three-armed star polypeptides, linear polypeptides, and their mixtures. These biosynthesized polypeptides have precise lengths and amino acid sequences. Transition temperatures were measured as a function of molecular weight and solution concentration and compared to their linear counterparts. Like their linear counterparts, the transition temperature is linearly related to log concentration. A mathematical relationship was used to fit the transition temperature data of different polypeptide lengths to a volume-based concentration using the polymer coil volume. The results of this model suggest that the linear ELP is in a random coil conformation at the transition temperature while the three-armed ELP is in a compact extended coil conformation, consistent with different pathways for aggregation. Solutions containing both trimer and linear constructs have two transition temperatures, further supporting differing aggregation behaviors. |
| Databáze: | OpenAIRE |
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