In-situ spectroscopic investigation of ultrasonic assisted unfolding and aggregation of insulin |
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Authors: | Helge Pfeiffer Nikos Chatziathanasiou Bert Verstraeten Filip Meersman Christ Glorieux Karel Heremans Martine Wevers |
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Affiliation: | 1. Department of Metallurgy and Materials Engineering, Group Material Performance and Non-destructive Testing, Katholieke Universiteit Leuven, Kasteelpark Arenberg 44, B-3001 Leuven, Belgium;2. Department of Chemistry, Unit of Molecular and Nanomaterials, Katholieke Universiteit Leuven, Celestijnenlaan 200G, B-3001 Leuven, Belgium;3. Department of Physics, Acoustic and Thermal Physics Section, Katholieke Universiteit Leuven, Celestijnenlaan 200G, B-3001 Leuven, Belgium;4. Department of Chemistry and Materials Chemistry Centre, Christopher Ingold Laboratories, University College London, 20 Gordon Street, London WC1H 0AJ, UK |
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Abstract: | It is well-known that fibrillogenesis of proteins can be influenced by diverse external parameters, such as temperature, pressure, agitation or chemical agents. The present preliminary study suggests that ultrasonic excitation at moderate intensities has a significant influence on the unfolding and aggregation behaviour of insulin. Irradiation with an average sound intensity of even as low as 70 mW/cm2 leads to a lowering of the unfolding and aggregation temperature up to 7 K. The effect could be explained by an increase of the aggregation kinetics due to ultrasonically induced acoustic micro-streaming in the insulin solution that most probably enhances the aggregation rate. The clear and remarkable effect at relatively low sound intensities offers interesting options for further applications of ultrasound in biophysics and biochemistry. On the other hand, a process that causes a change of kinetics equivalent to 7 K also gives a warning signal concerning the safety of those medical ultrasonic devices that work in this intensity range. |
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Keywords: | Fibrillogenesis Insulin Ultrasound Fourier transform infrared spectroscopy Atomic force microscopy Aggregation |
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