Rotational diffusion analysis of polyethylene glycol induced protein interactions

Daisuke Takahashi; Shoji Yamashita; Om Prakash; Etsuko Nishimoto

doi:10.1021/jp205279k

Rotational diffusion analysis of polyethylene glycol induced protein interactions

Daisuke Takahashi, Shoji Yamashita, Om Prakash, Etsuko Nishimoto

Molecular Biosciences

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3 Citations (Scopus)

Abstract

Protein intermolecular depletion interactions induced by polyethylene glycol (PEG) depend largely on its concentration and molecular weight. Herein, we investigated the effects of various concentrations and molecular weights of PEG on lysozyme interactions through the analysis of protein rotational diffusion, which is susceptible to intermolecular interactions at short range. To this end, we measured fluorescence anisotropy of fluorescein-tagged lysozyme added as a tracer in concentrated native lysozyme solutions and introduced a protein concentration-dependent interaction parameter, k_rot. The results show the nonmonotonic changes in k_rot as the concentrations of PEG10000 and 6000 are increased. The depletion attractions are characterized by the decrease in k_rot, indicating an increase of a degree at which protein rotational diffusion slows down. The influences of temperature on the lysozyme rotational diffusion and k_rot were also measured, and the validity of this approach was checked through comparison with the colloidal theory.

Original language	English
Pages (from-to)	11786-11792
Number of pages	7
Journal	Journal of Physical Chemistry B
Volume	115
Issue number	41
DOIs	https://doi.org/10.1021/jp205279k
Publication status	Published - Oct 20 2011

All Science Journal Classification (ASJC) codes

Physical and Theoretical Chemistry
Surfaces, Coatings and Films
Materials Chemistry

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title = "Rotational diffusion analysis of polyethylene glycol induced protein interactions",

abstract = "Protein intermolecular depletion interactions induced by polyethylene glycol (PEG) depend largely on its concentration and molecular weight. Herein, we investigated the effects of various concentrations and molecular weights of PEG on lysozyme interactions through the analysis of protein rotational diffusion, which is susceptible to intermolecular interactions at short range. To this end, we measured fluorescence anisotropy of fluorescein-tagged lysozyme added as a tracer in concentrated native lysozyme solutions and introduced a protein concentration-dependent interaction parameter, krot. The results show the nonmonotonic changes in krot as the concentrations of PEG10000 and 6000 are increased. The depletion attractions are characterized by the decrease in krot, indicating an increase of a degree at which protein rotational diffusion slows down. The influences of temperature on the lysozyme rotational diffusion and krot were also measured, and the validity of this approach was checked through comparison with the colloidal theory.",

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T1 - Rotational diffusion analysis of polyethylene glycol induced protein interactions

AU - Takahashi, Daisuke

AU - Yamashita, Shoji

AU - Prakash, Om

AU - Nishimoto, Etsuko

PY - 2011/10/20

Y1 - 2011/10/20

N2 - Protein intermolecular depletion interactions induced by polyethylene glycol (PEG) depend largely on its concentration and molecular weight. Herein, we investigated the effects of various concentrations and molecular weights of PEG on lysozyme interactions through the analysis of protein rotational diffusion, which is susceptible to intermolecular interactions at short range. To this end, we measured fluorescence anisotropy of fluorescein-tagged lysozyme added as a tracer in concentrated native lysozyme solutions and introduced a protein concentration-dependent interaction parameter, krot. The results show the nonmonotonic changes in krot as the concentrations of PEG10000 and 6000 are increased. The depletion attractions are characterized by the decrease in krot, indicating an increase of a degree at which protein rotational diffusion slows down. The influences of temperature on the lysozyme rotational diffusion and krot were also measured, and the validity of this approach was checked through comparison with the colloidal theory.

AB - Protein intermolecular depletion interactions induced by polyethylene glycol (PEG) depend largely on its concentration and molecular weight. Herein, we investigated the effects of various concentrations and molecular weights of PEG on lysozyme interactions through the analysis of protein rotational diffusion, which is susceptible to intermolecular interactions at short range. To this end, we measured fluorescence anisotropy of fluorescein-tagged lysozyme added as a tracer in concentrated native lysozyme solutions and introduced a protein concentration-dependent interaction parameter, krot. The results show the nonmonotonic changes in krot as the concentrations of PEG10000 and 6000 are increased. The depletion attractions are characterized by the decrease in krot, indicating an increase of a degree at which protein rotational diffusion slows down. The influences of temperature on the lysozyme rotational diffusion and krot were also measured, and the validity of this approach was checked through comparison with the colloidal theory.

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Rotational diffusion analysis of polyethylene glycol induced protein interactions

Abstract

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