Literature DB >> 28752485

Effect of Aggregation on the Hydrodynamic Properties of Bovine Serum Albumin.

Mariya A Pindrus1, James L Cole2, Japneet Kaur3, Steven J Shire4, Sandeep Yadav4, Devendra S Kalonia3.   

Abstract

PURPOSE: To systematically analyze shape and size of soluble irreversible aggregates and the effect of aggregate formation on viscosity.
METHODS: Online light scattering, refractive index and viscosity detectors attached to HPLC (Viscotek®) were used to study aggregation, molecular weight and intrinsic viscosity of bovine serum albumin (BSA). Irreversible aggregates were generated by heat stress. Bulk viscosity was measured by an oscillating piston viscometer.
RESULTS: As BSA was heated at a higher concentration or for a longer time, the relative contribution, molecular weight and intrinsic viscosity of aggregate species increased. Molecular shape was evaluated from intrinsic viscosity values, and aggregates were estimated to be more asymmetric than monomer species. The presence of aggregates resulted in an increase in bulk viscosity when relative contribution of very high molecular weight species exceeded 10%.
CONCLUSIONS: For model system and conditions studied, generation of higher order aggregate species was concluded to be associated with an increase in molecular asymmetry. Elevated viscosity in the presence of aggregated species points to molecular asymmetry being a critical parameter affecting solution viscosity of BSA.

Entities:  

Keywords:  aggregation; effective molecular shape; intrinsic viscosity

Mesh:

Substances:

Year:  2017        PMID: 28752485     DOI: 10.1007/s11095-017-2231-2

Source DB:  PubMed          Journal:  Pharm Res        ISSN: 0724-8741            Impact factor:   4.200


  27 in total

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4.  On the hydrodynamic analysis of macromolecular conformation.

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5.  VISCOSITY AND THE SHAPE OF PROTEIN MOLECULES.

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Review 6.  The intrinsic viscosity of biological macromolecules. Progress in measurement, interpretation and application to structure in dilute solution.

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7.  Classification and characterization of therapeutic antibody aggregates.

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8.  Do clustering monoclonal antibody solutions really have a concentration dependence of viscosity?

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9.  Protein aggregates seem to play a key role among the parameters influencing the antigenicity of interferon alpha (IFN-alpha) in normal and transgenic mice.

Authors:  A Braun; L Kwee; M A Labow; J Alsenz
Journal:  Pharm Res       Date:  1997-10       Impact factor: 4.200

10.  Characterization of particles in protein solutions: reaching the limits of current technologies.

Authors:  Barthélemy Demeule; Steven Messick; Steven J Shire; Jun Liu
Journal:  AAPS J       Date:  2010-10-16       Impact factor: 4.009

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  1 in total

1.  Protein Dielectrophoresis: I. Status of Experiments and an Empirical Theory.

Authors:  Ralph Hölzel; Ronald Pethig
Journal:  Micromachines (Basel)       Date:  2020-05-22       Impact factor: 2.891

  1 in total

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