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BrianWerry_Thesis_2013.pdf (1.77 MB)

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Characterizing Bile Acid Association as a Ligand and in Micellization.

Werry, Brian Scott
http://rave.ohiolink.edu/etdc/view?acc_num=case1386186690

Abstract Details

2014, Doctor of Philosophy, Case Western Reserve University, Chemistry.
Bile acids are an integral part of digestion and nutritional balance. Their role within physiology is influenced by their unique amphiphilic structure and their ability to associate into micelles in solution. The work herein presents an experimental analysis of the associative properties of the secondary bile acid, lithocholic acid (LCA), to human fatty acid binding protein 6 (hFABP6), a bile acid binding protein found exclusively in the ileum enterocytes. The analysis was conducted through a binding energetics study using isothermal titration calorimetry (ITC) and a binding-site selective study using a two-dimensional NMR spectroscopic binding site assay method. While LCA exhibited no binding to hFABP6 when alone, it bound with high positive cooperative affinity when in solution with cholic acid (CA). Interestingly, LCA had the highest cooperative binding affinity out of all the bile acid mixtures tested. The self-association of bile acids was also investigated. A statistical comparison of micellization models with differing definitions of micelle size dispersity was conducted using ITC. A bi-micelle multimer model was identified as the best model for fitting calorimetric data from bile acid demicellization studies, and it is suggested as a standard model for all bile acid self-association studies. Application of this standard model was then demonstrated through its use in fitting calorimetric data and calculation of thermodynamic values for bile acids of varying side chain lengths. The results were used in identifying significant properties for the C24 bile acids, which showed a physiological balance between function as detergents and cytosolic solubility with free energy values of ¿Gdimerization = -559.21 cal/mol and ¿Goctamerization = -2188.62 cal/mol.
Gregory Tochtrop (Advisor)
149 p.
Chemistry; Organic Chemistry
bile acids, bile salts, micellization, micelle, association, FABP6, IBABP, bile acid binding protein

Recommended Citations

Citations

  • Werry, B. S. (2014). Characterizing Bile Acid Association as a Ligand and in Micellization. [Doctoral dissertation, Case Western Reserve University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=case1386186690

    APA Style (7th edition)

  • Werry, Brian. Characterizing Bile Acid Association as a Ligand and in Micellization. 2014. Case Western Reserve University, Doctoral dissertation. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=case1386186690.

    MLA Style (8th edition)

  • Werry, Brian. "Characterizing Bile Acid Association as a Ligand and in Micellization." Doctoral dissertation, Case Western Reserve University, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=case1386186690

    Chicago Manual of Style (17th edition)

case1386186690
690
© 2014, some rights reserved.Creative Commons License Characterizing Bile Acid Association as a Ligand and in Micellization. by Brian Scott Werry is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported License. Based on a work at etd.ohiolink.edu.
This open access ETD is published by Case Western Reserve University School of Graduate Studies and OhioLINK.