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Rigidity of poly‐ L ‐glutamic acid scaffolds: Influence of secondary and supramolecular structure
Author(s) -
Nickels Jonathan D.,
Perticaroli Stefania,
Ehlers Georg,
Feygenson Mikhail,
Sokolov Alexei P.
Publication year - 2015
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.35427
Subject(s) - materials science , supramolecular chemistry , rigidity (electromagnetism) , protein secondary structure , biomaterial , nanometre , structural rigidity , hydrogen bond , intermolecular force , nanotechnology , scaffold , chemical engineering , crystallography , composite material , molecule , organic chemistry , chemistry , biomedical engineering , crystal structure , medicine , biochemistry , geometry , mathematics , engineering
Poly‐ l ‐glutamic acid (PGA) is a widely used biomaterial, with applications ranging from drug delivery and biological glues to food products and as a tissue engineering scaffold. A biodegradable material with flexible conjugation functional groups, tunable secondary structure, and mechanical properties, PGA has potential as a tunable matrix material in mechanobiology. Recent studies in proteins connecting dynamics, nanometer length scale rigidity, and secondary structure suggest a new point of view from which to analyze and develop this promising material. We have characterized the structure, topology, and rigidity properties of PGA prepared with different molecular weights and secondary structures through various techniques including scanning electron microscopy, FTIR, light, and neutron scattering spectroscopy. On the length scale of a few nanometers, rigidity is determined by hydrogen bonding interactions in the presence of neutral species and by electrostatic interactions when the polypeptide is negatively charged. When probed over hundreds of nanometers, the rigidity of these materials is modified by long range intermolecular interactions that are introduced by the supramolecular structure. © 2015 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 103A: 2909–2918, 2015.