Semicrystalline Lysine Functionalized Precision Polyolefins

Authors

  • James K. Leonard,

    1. The George and Josephine Butler Polymer Research Laboratory University of Florida, Gainesville, Florida 32611, USA
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  • Timothy E. Hopkins,

    1. The George and Josephine Butler Polymer Research Laboratory University of Florida, Gainesville, Florida 32611, USA
    2. 215 West Pembrey Drive, Wilmington, Delaware 19803; USA
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  • Kim Chaffin,

    1. The George and Josephine Butler Polymer Research Laboratory University of Florida, Gainesville, Florida 32611, USA
    2. Medtronic, Inc., Minneapolis, Minnesota 55432, USA
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  • Kenneth B. Wagener

    Corresponding author
    1. The George and Josephine Butler Polymer Research Laboratory University of Florida, Gainesville, Florida 32611, USA
    • The George and Josephine Butler Polymer Research Laboratory University of Florida, Gainesville, Florida 32611, USA.
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Abstract

A family of semicrystalline polymers with the amino acid lysine regularly and atactically attached along a polyethylene backbone has been prepared via metathesis polymerization. The lysine branches are placed precisely on every 21st carbon of the polyethylene backbone giving these polymers a perfectly known architecture. Attachment of the amino acid is varied either by using a succinic acid spacer or directionally through its C- or N-terminus. Changes in physical and spectral properties are discussed as a direct consequence of the nature of the amino acid connection and structure. The crystallinity of these polymers is studied by differential scanning calorimetry (DSC) and wide angle X-ray scattering (WAXS), where it has become clear that the crystalline unit cell resembles that of the pure monomer. Long range order was absent as shown by small angle X-ray scattering (SAXS). Complete deprotection of the amine branch of the lysine moiety of one polymer is discussed both in terms of procedure and its subsequent effect on the material's crystallinity.

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