Stability of helix-rich proteins at high concentrations

Stability of helix-rich proteins at high concentrations
Engineering Village 2
? 2006 Elsevier Inc
Accession number: 063010023241

Title: Stability of helix-rich proteins at high concentrations

Authors: Guo, Jianxin; Harn, Nicholas; Robbins, Aaron; Dougherty, Ron; Middaugh, C. Russell

Author affiliation: Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, KS 66047, United States

Serial title: Biochemistry

Abbreviated serial title: Biochemistry

Volume: v 45

Issue: n 28

Issue date: Jul 18 2006

Publication year: 2006

Pages: p 8686-8696

Language: English

ISSN: 0006-2960


Document type: Journal article (JA)

Publisher: American Chemical Society, Columbus, OH 43210-3337, United States

Abstract: A number of techniques, including circular dichroism, FTIR, front face fluorescence, and UV absorption spectrophotometries, dynamic light scattering, and DSC, were used to directly measure the colloidal and conformational stability of proteins in highly concentrated solutions. Using bovine serum albumin (BSA), chicken egg white lysozyme, human hemoglobin A0, and bovine fibrinogen as model proteins, the thermal transition temperatures of proteins in dilute and concentrated solutions were compared. At 10 ?C, no significant differences in both secondary and tertiary structures were detected for proteins at different concentrations. When temperature was introduced as a variable, however, hemoglobin and fibrinogen demonstrated higher transition midpoints (Tms) in concentrated rather than in dilute solutions (?Tm [similar to] 2-10 ?C). In contrast, lysozyme and BSA in concentrated solutions exhibit a lower Tm than in dilute solutions (?Tm [similar to] 2-20 ?C). From these studies, it appears that a variety of factors determine the effect of high concentrations on the colloidal and conformational stability of a particular protein. While the prediction of excluded volume theory is that high concentrations should conformationally stabilize proteins, other factors such as pH, kinetics, protein dynamics, and intermolecular charge-charge effects may affect the overall stability of proteins at high concentrations under certain conditions. ? 2006 American Chemical Society.

Number of references: 35

Ei main heading: Proteins

Ei controlled terms: Concentration (process) - Fluorescence - Conformations - Thermal effects - Fourier transform infrared spectroscopy - Differential scanning calorimetry

Uncontrolled terms: Helix-rich proteins - Concentrated solutions - Thermal transition temperature - Charge-charge effects

Ei classification codes: 804.1 Organic Compounds - 802.3 Chemical Operations - 741.1 Light/Optics - 801.4 Physical Chemistry - 921.4 Combinatorial Mathematics, Includes Graph Theory, Set Theory - 931.1 Mechanics - 944.6 Temperature Measurements

Treatment: Theoretical (THR); Experimental (EXP)

DOI: 10.1021/bi060525p

Database: Compendex

Compilation and indexing terms, ? 2006 Elsevier Inc. All rights reserved
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