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QUANTIFYING THE BIOMECHANICAL FORCES BETWEEN PROTEINS INVOLVED IN ELASTIN SYNTHESIS USING ATOMIC FORCE MICROSCOPY

Moore, Sean O'Neill
http://orcid.org/0000-0002-2079-4229
http://rave.ohiolink.edu/etdc/view?acc_num=csu1546450170942598

Abstract Details

2018, Master of Science in Biomedical Engineering, Cleveland State University, Washkewicz College of Engineering.
Elastogenesis is a complex and arduous process involving a series of biochemical and biomechanical interactions, from extraction of precursor proteins out of cells to cross-linking and deposition, ultimately forming elastic fibers. Elastin is an extracellular matrix protein comprised of two main proteins, tropoelastin and fibrillin-1, which gives tissues and organs resilience and elasticity under deformation. While the biochemical process by which elastic fibers are assembled is being elucidated, the forces between the constituents involved in this process remains unknown. To fill this knowledge gap in literature, this study measured and quantified the adhesive forces between elastic fiber components, primarily between tropoelastin, elastin binding protein (EBP), fibrillin-1, fibulin-5, and lysyl oxidase (LOX). The forces between other extracellular matrix proteins such as laminin-1, rat-tail collagen type I, and human collagen type I were also measured using atomic force microscopy (AFM). The interactions between an uncoated AFM cantilever tip with proteins (involved in elastin synthesis) coated on a cover glass showed that the adhesive forces increased with increasing molecular weight of the proteins. The adhesive forces between elastin synthesis proteins when tropoelastin was coated on the AFM cantilever tip revealed the strongest interaction to be when tropoelastin was coated on the cover glass (293.4 ± 20.5 pN), followed by LOXL2, fibulin-5, fibrillin-1, GLB-1, and mature elastin, which ranged between 100.3 pN to 199.8 pN. Introducing the cross-linker protein, LOXL2, decreased the adhesive force between the tropoelastin-coated AFM tip and tropoelastin-coated cover glass by roughly 100 pN. Lastly, the Worm-Like Chain (WLC) model provided insights into the bending rigidity, stiffness, and flexibility of elastin synthesis proteins as they were unfolding. This gives understanding to how each protein’s stretching capabilities under deformation contribute to elastin’s overall elastic nature. Knowing the forces between the individual molecules in elastogenesis could help understand their contributions to elastic matrix deposition and assembly, thereby the interactions between cells and extracellular matrix (ECM) components. This study led to bridging the gap between biochemical information and biomechanics, pertaining to elastic fiber assembly.
Chandrasekhar Kothapalli, PhD (Advisor)
Nolan Holland, PhD (Committee Member)
Jason Halloran, PhD (Committee Member)
92 p.
Biomedical Engineering

Recommended Citations

Citations

  • Moore, S. O. (2018). QUANTIFYING THE BIOMECHANICAL FORCES BETWEEN PROTEINS INVOLVED IN ELASTIN SYNTHESIS USING ATOMIC FORCE MICROSCOPY [Master's thesis, Cleveland State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=csu1546450170942598

    APA Style (7th edition)

  • Moore, Sean. QUANTIFYING THE BIOMECHANICAL FORCES BETWEEN PROTEINS INVOLVED IN ELASTIN SYNTHESIS USING ATOMIC FORCE MICROSCOPY . 2018. Cleveland State University, Master's thesis. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=csu1546450170942598.

    MLA Style (8th edition)

  • Moore, Sean. "QUANTIFYING THE BIOMECHANICAL FORCES BETWEEN PROTEINS INVOLVED IN ELASTIN SYNTHESIS USING ATOMIC FORCE MICROSCOPY ." Master's thesis, Cleveland State University, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=csu1546450170942598

    Chicago Manual of Style (17th edition)

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This open access ETD is published by Cleveland State University and OhioLINK.