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Characterization of Elastin-like Polypeptide Micelles Using Capillary Viscometry

Kambow, Sumit H.
http://rave.ohiolink.edu/etdc/view?acc_num=csu1337605892

Abstract Details

2012, Master of Science in Chemical Engineering, Cleveland State University, Fenn College of Engineering.
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 foldon, has a net negative charge and behaves as a hydrophilic group to stabilize the aggregates formed by the ELP chains above their transition temperature. The coacervate, which makes up interior of micelles, contains 37% protein and 63% water when it is in a bulk state. The aim of my research was to find out the density of protein in the micelle by using capillary viscometry. We used Ubbelohde capillary viscometer to calculate the relative viscosity of ELPs which was used to calculate the intrinsic viscosities using Kraemer and Huggins equations. The micelles at low salt concentration and high pH are spherical therefore we use equivalent sphere model to calculate the density of protein per micelle from intrinsic viscosity. Using this model we calculated the density of protein per micelle to be 0.26 g/ ml. Using our micelle model and data from light scattering, we calculated the density of protein in the coacervate to be 40% and rest water. There were two limitations in this project. First, specific viscosities at low concentrations were small with large errors. The second limitation was controlling the pH of the polymer solutions during the experiments. The pH of polymer solution could not easily be monitored once the sample was loaded in the viscometer.
Nolan Holland, PhD (Advisor)
Rolf Lustig, PhD (Committee Member)
Dhananjai Shah, PhD (Committee Member)
67 p.
Biomedical Engineering; Biomedical Research; Chemical Engineering

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Citations

  • Kambow, S. H. (2012). Characterization of Elastin-like Polypeptide Micelles Using Capillary Viscometry [Master's thesis, Cleveland State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=csu1337605892

    APA Style (7th edition)

  • Kambow, Sumit. Characterization of Elastin-like Polypeptide Micelles Using Capillary Viscometry. 2012. Cleveland State University, Master's thesis. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=csu1337605892.

    MLA Style (8th edition)

  • Kambow, Sumit. "Characterization of Elastin-like Polypeptide Micelles Using Capillary Viscometry." Master's thesis, Cleveland State University, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=csu1337605892

    Chicago Manual of Style (17th edition)

csu1337605892
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© 2012, all rights reserved.
This open access ETD is published by Cleveland State University and OhioLINK.