Abstract
Defining precisely the mechanical properties of bio-macromolecular systems on a nanometer length scale is crucial for the development of more efficient drug delivery systems and scaffolds-based tissue engineering. We characterized the structure, topology, and rigidity properties of poly-L-glutamic acid (PGA), prepared with different molecular weights and secondary structures, using the same approach that we recently applied to proteins1-3. We employed various techniques, including FT-IR, SEM, light scattering, neutron diffraction, and neutron scattering spectroscopy. Our results show that on the length scale of a few nanometers, rigidity of PGA powders is determined by hydrogen bonding interactions in presence of neutral species, and by electrostatic interactions when the polypeptide is negatively charged. On ∼ a hundred nanometer length scale, the rigidity of these materials is modified by long range intermolecular interactions that are introduced in the supramolecular structures.1. Perticaroli, S. et. al. Biophys. J. 2014, 106, 2667.2. Perticaroli, S. et al. Soft Matter 2013, 9, 9548.3. Perticaroli, S. et al. J. Phys Chem. B 2014, 118, 7317.
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