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    Inhibition of Cell Adhesion by Peptides Derived from the EC-4 Domain of E-Cadherin

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    Behymer_ku_0099M_14162_DATA_1.pdf (1.225Mb)
    Issue Date
    2015-08-31
    Author
    Behymer, Matthew Mark
    Publisher
    University of Kansas
    Format
    34 pages
    Type
    Thesis
    Degree Level
    M.S.
    Discipline
    Pharmaceutical Chemistry
    Rights
    Copyright held by the author.
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    Abstract
    The objective of this project was to evaluate the biological activity of peptides derived from the EC-4 domain of E-cadherin in inhibiting E-cadherin-mediated cell-cell adhesion. The activity of these peptides was determined by inhibition of Caco-2 single cells that bind to a Caco-2 monolayer and inhibition of junction resealing of MDCK II cell monolayers. The results showed that peptide 6 (LVVQAADLQG) derived from the EC-2 domain and peptide 8 derived from the EC-4 domain (YTALIIATDN) of E-cadherin were more effective in inhibiting single cell adhesion than peptides from other domains (EC-1, EC-3) of E-cadherin. Peptide 8 had better activity than peptide 6. From overlapping hexapeptides derived from peptide 8, it was found that peptide 12 with ALIIAT sequence had the best activity, suggesting that it was the activity sequence of peptide 8. Alanine-scanning and mutation experiments found that peptide 22 (TEIIAT) had the best activity compared to other hexapeptides derived from peptide 8 in inhibiting cell adhesion of Caco-2 cells and junction resealing of MDCK-II cell monolayers.
    URI
    http://hdl.handle.net/1808/21666
    Collections
    • Pharmaceutical Chemistry Dissertations and Theses [141]
    • Theses [3797]

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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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