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Title: Rigidity of poly-L-glutamic acid scaffolds: Influence of secondary and supramolecular structure

Abstract

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. Some 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. Our paper characterizes 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. Finally, 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.

Authors:
 [1];  [1];  [2];  [2];  [1]
  1. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); Univ. of Tennessee, Knoxville, TN (United States)
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1261462
DOE Contract Number:  
AC05-00OR22725
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of Biomedical Materials Research. Part A; Journal Volume: 103; Journal Issue: 9
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; 36 MATERIALS SCIENCE; neutron and light scattering; tissue engineering; boson peak; elastic modulus; mechanobiology nanomechanical; TITIN IMMUNOGLOBULIN DOMAINS; PLURIPOTENT STEM-CELLS; POLY(L-GLUTAMIC ACID); NEUTRON-SCATTERING; BETA-SHEET; SOUND-VELOCITY; PROTEIN

Citation Formats

Nickels, Jonathan D., Perticaroli, Stefania, Ehlers, Georg, Feygenson, Mikhail, and Sokolov, Alexei P. Rigidity of poly-L-glutamic acid scaffolds: Influence of secondary and supramolecular structure. United States: N. p., 2015. Web. doi:10.1002/jbm.a.35427.
Nickels, Jonathan D., Perticaroli, Stefania, Ehlers, Georg, Feygenson, Mikhail, & Sokolov, Alexei P. Rigidity of poly-L-glutamic acid scaffolds: Influence of secondary and supramolecular structure. United States. doi:10.1002/jbm.a.35427.
Nickels, Jonathan D., Perticaroli, Stefania, Ehlers, Georg, Feygenson, Mikhail, and Sokolov, Alexei P. Thu . "Rigidity of poly-L-glutamic acid scaffolds: Influence of secondary and supramolecular structure". United States. doi:10.1002/jbm.a.35427.
@article{osti_1261462,
title = {Rigidity of poly-L-glutamic acid scaffolds: Influence of secondary and supramolecular structure},
author = {Nickels, Jonathan D. and Perticaroli, Stefania and Ehlers, Georg and Feygenson, Mikhail and Sokolov, Alexei P.},
abstractNote = {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. Some 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. Our paper characterizes 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. Finally, 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.},
doi = {10.1002/jbm.a.35427},
journal = {Journal of Biomedical Materials Research. Part A},
number = 9,
volume = 103,
place = {United States},
year = {Thu Jan 01 00:00:00 EST 2015},
month = {Thu Jan 01 00:00:00 EST 2015}
}