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Laser interferometry of the hydrolytic changes in protein solutions: the refractive index and hydration shells

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Abstract

Using an original laser interferometer of enhanced sensitivity, an increase in the refractive index of a protein solution was observed during the reaction of proteolysis catalyzed by pepsin. The increase in the refractive index of the protein solution at a concentration of 4 mg/ml was \( 9 \times 10^{-6} \) for bovine serum albumin and \(2.4 \times 10^{- 6}\) for lysozyme. The observed effect disproves the existing idea that the refractive index of protein solutions is determined only by their amino acid composition and concentration. It is shown that the refractive index also depends on the state of protein fragmentation. A mathematical model of proteolysis and a real-time method for estimating the state of protein hydration based on the measurement of refractive index during the reaction are proposed. A good agreement between the experimental and calculated time dependences of the refractive index shows that the growth of the surface of protein fragments and the change in the number of hydration cavities during proteolysis can be responsible for the observed effect.

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Authors and Affiliations

  1. Prokhorov General Physics Institute of the Russian Academy of Sciences, GPI RAS, 38 Vavilov str., 119991, Moscow, Russia

    R. M. Sarimov, T. A. Matveyeva & V. N. Binhi

  2. Faculty of Biology, Lomonosov Moscow State University, 1-12 Leninskie Gory, 119991, Moscow, Russia

    V. N. Binhi

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  1. R. M. Sarimov
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Correspondence to R. M. Sarimov.

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Sarimov, R.M., Matveyeva, T.A. & Binhi, V.N. Laser interferometry of the hydrolytic changes in protein solutions: the refractive index and hydration shells. J Biol Phys 44, 345–360 (2018). https://doi.org/10.1007/s10867-018-9494-7

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  • DOI: https://doi.org/10.1007/s10867-018-9494-7

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