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Title: Short-Time Glassy Dynamics in Viscous Protein Solutions with Competing Interactions

Journal Article · · Physical Review Letters
 [1];  [2];  [3];  [4];  [4];  [1];  [2]
  1. Univ. of Delaware, Newark, DE (United States)
  2. National Inst. of Standards and Technology (NIST), Gaithersburg, MD (United States)
  3. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
  4. Inst. Laue-Langevin (ILL), Grenoble (France)

Although there have been numerous investigations of the glass transition for colloidal dispersions with only a short-ranged attraction, less is understood for systems interacting with a long-ranged repulsion in addition to this attraction, which is ubiquitous in aqueous protein solutions at low ionic strength. Highly puri ed concentrated lysozyme solutions are used as a model system and investigated over a large range of protein concentrations at very low ionic strength. Newtonian liquid behavior is observed at all concentrations, even up to 480 mg/mL, where the zero shear viscosity increases by more than three orders of magnitude with increasing concentration. Remarkably, despite this macroscopic liquid-like behavior, the measurements of the dynamics in the short-time limit shows features typical of glassy colloidal systems. Investigation of the inter-protein structure indicates that the reduced short-time mobility of the protein is caused by localized regions of high density within a heterogeneous density distribution. This structural heterogeneity occurs on intermediate range length scale, driven by the competing potential features, and is distinct from commonly studied colloidal gel systems in which a heterogeneous density distribution tends to extend to the whole system. The presence of long-ranged repulsion also allows for more mobility over large length and long time scales resulting in the macroscopic relaxation of the structure. The experimental results provide evidence for the need to explicitly include intermediate range order in theories for the macroscopic properties of protein solutions interacting via competing potential features.

Research Organization:
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). Center for Nanophase Materials Sciences (CNMS)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
Grant/Contract Number:
AC05-00OR22725
OSTI ID:
1286934
Alternate ID(s):
OSTI ID: 1227033
Journal Information:
Physical Review Letters, Vol. 115, Issue 22; ISSN 0031-9007
Publisher:
American Physical Society (APS)Copyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 55 works
Citation information provided by
Web of Science

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Cited By (8)

Short-time dynamics of lysozyme solutions with competing short-range attraction and long-range repulsion: Experiment and theory journal February 2018
Multi-attribute PAT for UF/DF of Proteins—Monitoring Concentration, particle sizes, and Buffer Exchange journal February 2020
Investigating the effective interaction between silica colloidal particles near the critical point of a binary solvent by small angle neutron scattering journal August 2018
Dynamic cluster formation determines viscosity and diffusion in dense protein solutions journal April 2019
Recovery, overloading, and protein interactions in asymmetrical flow field-flow fractionation journal February 2019
Dynamics of proteins in solution journal January 2019
Microliter viscometry using a bright-field microscope: η -DDM journal January 2018
Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions journal December 1998

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