Ultrasonic investigation of the conformal changes of bovine serum albumin in aqueous solution

Kessler, L. W.; Dunn, F.

doi:10.1021/j100846a037

Cited by 50 publications

(13 citation statements)

References 3 publications

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“…This could be due to a different level of coordination between the lysozyme aggregated species or to their different structure and/or dimensions. Our outcomes were in agreement with previous studies on other protein solutions [16,27]. The authors found that the protein's conformational rearrangements and the aggregate's formation highly affect the attenuation of the acoustic waves.…”

Section: Appl Sci 2019 9 X For Peer Review 6 Of 11supporting

confidence: 93%

“…In particular, C. M. Bryant and D. J. McClements [16] study the behavior of the acoustic wave through a solution of whey proteins, finding that the acoustic attenuation in protein solutions is due both to scattering contributions and protein relaxation phenomena. The latter could be related to hydration, proton transfer [23][24][25] and conformational changes [26,27]. Despite several studies on this argument, one of the major challenges of research in the field of soft matter remains that of relating intra-and intermolecular interactions that govern the structure of individual proteins and their aggregates with the elastic macroscopic characteristics of the whole system.…”

Section: Introductionmentioning

confidence: 99%

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Probing Globular Protein Self-Assembling Dynamics by Heterodyne Transient Grating Experiments

et al. 2019

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In this work, we studied the propagation of ultrasonic waves of lysozyme solutions characterized by different degrees of aggregation and networking. The experimental investigation was performed by means of the transient grating (TG) spectroscopy as a function of temperature, which enabled measurement of the ultrasonic acoustic proprieties over a wide time window, ranging from nanoseconds to milliseconds. The fitting of the measured TG signal allowed the extraction of several dynamic properties, here we focused on the speed and the damping rate of sound. The temperature variation induced a series of processes in the lysozyme solutions: Protein folding-unfolding, aggregation and sol–gel transition. Our TG investigation showed how these self-assembling phenomena modulate the sound propagation, affecting both the velocity and the damping rate of the ultrasonic waves. In particular, the damping of ultrasonic acoustic waves proved to be a dynamic property very sensitive to the protein conformational rearrangements and aggregation processes.

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Section: Appl Sci 2019 9 X For Peer Review 6 Of 11supporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Probing Globular Protein Self-Assembling Dynamics by Heterodyne Transient Grating Experiments

et al. 2019

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“…The phase transitions that can occur in biological membranes are very diverse (Georgescauld et al 1979;Hazel et al 1998;Koynova and Caffrey 1998) and have timescales from ns to ms (Holzwarth 1989). Within that range of time scales, US has been shown to effect changes in the conformational state of single and multiple component lipid vesicles and proteins (Halstenberg et al 1998;Holzwarth 1989;Kessler and Dunn 1969;O'Brien Jr and Dunn 1972;Tatat and Dunn 1992). The mechanisms described here are related to processes by which US produces conformational changes, which will then result in nerve excitation.…”

Section: Mechanismsmentioning

confidence: 94%

Ultrasound Neuromodulation: A Review of Results, Mechanisms and Safety

Blackmore

Shrivastava

Sallet

et al. 2019

Ultrasound in Medicine & Biology

377

285

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Ultrasonic neuromodulation is a rapidly growing field, in which low-intensity ultrasound (US) is delivered to nervous system tissue, resulting in transient modulation of neural activity. This review summarizes the findings in the central and peripheral nervous systems from mechanistic studies in cell culture to cognitive behavioral studies in humans. The mechanisms by which US mechanically interacts with neurons and could affect firing are presented. An in-depth safety assessment of current studies shows that parameters for the human studies fall within the safety envelope for US imaging. Challenges associated with accurately targeting US and monitoring the response are described. In conclusion, the literature supports the use of US as a safe, non-invasive brain stimulation modality with improved spatial localization and depth targeting compared with alternative methods. US neurostimulation has the potential to be used both as a scientific instrument to investigate brain function and as a therapeutic modality to modulate brain activity.

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“…As noted above, ultrasonic absorption (UA) spectroscopy is a unique tool, suitable for studying dynamic processes of protein related to energy dissipation. For this purpose we have studied the effect of various viscous cosolvents on the UA of bovine serum albumin, a globular protein that has been well characterized by UA (29)(30)(31)(32).…”

Section: Introductionmentioning

confidence: 99%

Viscous cosolvent effect on the ultrasonic absorption of bovine serum albumin

Almagor¹,

Yedgar²,

Gavish³

1992

Biophysical Journal

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Protein-ligand binding and enzyme activity have been shown to be regulated by solvent viscosity, induced by the addition of viscous cosolvents. This was indirectly interpreted as an effect on protein dynamics. However, viscous cosolvents might affect dynamic, e.g., viscosity, as well as thermodynamic properties of the solution, e.g., activity of solution components. This work was undertaken to examine the effect of viscous cosolvent on the structural dynamics of proteins and its correlation with dynamic and thermodynamic solution properties. For this purpose we studied the effect of viscous cosolvent on the specific ultrasonic absorption, delta mu, of bovine serum albumin, at pH = 7.0 and at 21 degrees C, and frequency range of 3-4 MHz. Ultrasonic absorption (UA) directly probes protein dynamics related to energy dissipation processes. It was found that the addition of sucrose, glycerol, or ethylene glycol increased the BSA delta mu. This increase correlates well with the solvent viscosity, but not with the cosolvent mass concentration, activity of the solvent components, dielectric constant, or the hydration of charged groups. On the grounds of these results and previously reported findings, as well as theoretical considerations, we propose the following mechanism for the solvent viscosity effect on the protein structural fluctuations, reflected in the UA: increased solvent viscosity alters the frequency spectrum of the polypeptide chain movements; attenuating the fast (small amplitude) movements, and enhancing the slow (large amplitude) ones. This modulates the interaction strength between the polypeptide and water species that "lubricates" the chain's movements, leading to larger protein-volume fluctuation and higher ultrasonic absorption. This study demonstrates that solvent viscosity is a regulator of protein structural fluctuations.

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Ultrasonic investigation of the conformal changes of bovine serum albumin in aqueous solution

Cited by 50 publications

References 3 publications

Probing Globular Protein Self-Assembling Dynamics by Heterodyne Transient Grating Experiments

Probing Globular Protein Self-Assembling Dynamics by Heterodyne Transient Grating Experiments

Ultrasound Neuromodulation: A Review of Results, Mechanisms and Safety

Viscous cosolvent effect on the ultrasonic absorption of bovine serum albumin

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