Session: Undergraduate Research in Polymer Science:

Amyloid peptide fibrils have the potential to enhance the biocompatibility and mechanical properties of materials for biomaterials applications. Due to their binding affinity to proteins, glycopolymers show great promise for the design of peptide-polymer biomaterials such as hydrogels. In this work, two synthetic amyloid peptides (DP7 and DP8) with varying amino acid sequences were analyzed using atomic force microscopy (AFM) to investigate the effects of amino acid sequence on amyloid fibril morphology. DP7 exhibited an average height of 4.5 nm and average diameter of 59.9 nm. DP8 exhibited an average height of 2.5 nm and an average diameter of 68.6 nm. Two acrylamide-based glycopolymers with stereospecific pendent groups of either β-D-glucose or β-D-galactose (PGlcEAm and PGalEAm) were synthesized using RAFT polymerization and characterized using gel permeation chromatography with multi-angle laser light scattering (GPC-MALLS) and proton NMR. Dynamic light scattering (DLS) was performed on the glycopolymer solutions to understand the effect of concentration on polymer chain aggregation in solution. PGalEAm exhibited concentration-dependent aggregation whereas PGlcEAm did not. Furthermore, PGalEAm exhibited aggregates with overall larger hydrodynamic diameters compared to PGlcEAm.

Sarah Morgan

University of Southern Mississippi

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