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Articles 1 - 4 of 4
Full-Text Articles in Biomedical Engineering and Bioengineering
Solute Partitioning In Elastin-Like Polypeptides: A Foundation For Drug Delivery Applications, Eric Helm
Solute Partitioning In Elastin-Like Polypeptides: A Foundation For Drug Delivery Applications, Eric Helm
ETD Archive
No abstract provided.
Synthesis And Characterization Of Ph-Responsive Elastin-Like Polypeptides With Different Configurations, Mingjie Tang
Synthesis And Characterization Of Ph-Responsive Elastin-Like Polypeptides With Different Configurations, Mingjie Tang
ETD Archive
Elastin-like polypeptides (ELP) are environmentally responsive polymers that exhibit phase transition behavior in response to various stimuli such as temperature, pH and irradiation. In this work, we focused on pH-responsive ELPs. It has been shown that pH value, configurations of ELPs, ELP concentration, and salt concentration can impact the phase transition behavior of pH-responsive ELPs. Quantitative models have been developed to engineer various linear ELPs, but there has not been any detailed study for engineering ionizable ELP with non-linear configurations. In this study, we designed, synthesized, and characterized pH-responsive ELPs with two different configurations. One is linear ELP, (GVGVPGEGVPGVGVP)12, and …
Characterization Of Elastic-Like Polypeptide Micelles Using Capillary Viscometry, Sumit H. Kambow
Characterization Of Elastic-Like Polypeptide Micelles Using Capillary Viscometry, Sumit H. Kambow
ETD Archive
Elastin-like polypeptides (ELPs) are a part of the family of responsive polymers. These polymers can be made to respond to a wide variety of stimuli, including temperature, pH, salt, concentration, light, and solvent. Elastin-like polypeptides are soluble in water at low temperatures but they become hydrophobic and insoluble above their transition temperature. Elastin-like polypeptides, (GVGVP)40-foldon and (GVGVP)60-foldon, were expressed in bacterial system. These ELPs above their transition temperature, Tt, at low salt (< 45mM) and high pH (> pH 10) assemble into micelles where the hydrophobic tails phase separate in the interior of the micelle as an immiscible coacervate phase. The oligomerization domain termed as …
Characterization Of Elastin-Like Polypeptides Using Viscometry, Hamdan Noman Alanazi
Characterization Of Elastin-Like Polypeptides Using Viscometry, Hamdan Noman Alanazi
ETD Archive
Elastin-like polypeptides (ELPs) are a class of polypeptide polymers that are gaining interest in various potential applications. These polymers are responsive to the changes in their environment by exhibiting conformational changes and aggregation. Monodisperse elastin-like polypeptides, (GVGVP)40, (GVGVP)40-foldon, and (GVGVP)60-foldon are made in bacterial expression system. An Ubbelohde capillary viscometer was set up to characterize the structural changes of these ELPs in phosphate buffered saline (PBS) solution. For the ELP-foldon, the relative viscosity measurements were utilized to calculate the intrinsic viscosities using Kraemer and Huggins equations. The known molecular weights of the ELPs and the experimentally determined intrinsic viscosities facilitated …