Mutual interactions in a ternary protein/bioprotectant/water system |
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| Institution: | 1. Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, Viale D’Alcontres 31, 98166, Messina, Italy;2. Laboratoire de Chimie Physique, UMR8000, Université Paris Sud, 91405, Orsay cedex, France;3. ISIS Facility, STFC Rutherford Appleton Laboratory, Chilton, Oxon, OX11 0QX, UK;4. Department of Chemistry and Biochemistry, Texas Tech University, Box 41061, Lubbock, TX 79409, USA;5. Theoretical Division, Los Alamos National Laboratory, Los Alamos, NM, 87545, USA;6. Department of Mathematical and Informatics Sciences, Physical Sciences and Earth Sciences, University of Messina, Viale D’Alcontres 31, 98166, Messina, Italy;1. Department of Chemistry ‘Ugo Schiff’, University of Florence, Scientific Campus, via della Lastruccia 3-13, 50019 Sesto F.no, Italy;2. European Laboratory for Non Linear Spectroscopy (LENS), University of Florence, Scientific Campus, via N. Carrara 1, 50019 Sesto F.no, Italy;3. Department of Photonics, Saint Petersburg Electrotechnical University, Ul. Professora Popova 5, 197376 St. Petersburg, Russia;1. Laboratório de Nanoestruturas Plasmônicas – LabNano, Departamento de Química, ICE, Universidade Federal de Juiz de Fora, 36036-900 Juiz de Fora, MG, Brazil;2. Museu de Arte Murilo Mendes, Universidade Federal de Juiz de Fora, 36036-900 Juiz de Fora, MG, Brazil;1. Key Laboratory of High-temperature and High-pressure Study of the Earth’s Interior, Institute of Geochemistry, Chinese Academy of Sciences, Guiyang, Guizhou 550081, China;2. University of Chinese Academy of Sciences, Beijing 100049, China;3. Institute of Earth Sciences, Academia Sinica, Taipei 115, Taiwan;1. Departamento de Física, Universidade Tecnológica Federal do Paraná, Campus Ponta Grossa, Avenida Monteiro Lobato 1787, 84.016-210, Ponta Grossa, Paraná, Brazil;2. Departamento de Física, Universidade Estadual de Ponta Grossa, Av. Gen. Carlos Cavalcanti 4748, 84.030-000, Ponta Grossa, Paraná, Brazil;1. Departamento de Engenharia da Computação, Universidade Federal do Ceará, CEP 62.010-560, Sobral, CE, Brazil;2. Departamento de Física, Universidade Federal do Ceará, P. O. Box 6030, CEP 60.455-970, Fortaleza, CE, Brazil;3. Departamento de Física, Campus Ministro Petrônio Portella, Universidade Federal do Piauí, CEP 64.049-550, Teresina, PI, Brazil |
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| Abstract: | The dynamics of hydration water play a key role in many biological processes. The activity and function of proteins are strongly affected by the presence of water, which interacts primarily by means of hydrogen bonding. These interactions are examined in this work by a comparison of neutron vibrational spectra (Inelastic Neutron Scattering, INS) of dry lysozyme and hydrated lysozyme at h = 0.7 (g of H2O/g of protein) with those of a lysozyme/water mixture at the same hydration value in the presence of the glass-forming bioprotectant trehalose. A difference spectrum, obtained by subtracting the dry lysozyme spectrum from that of the lysozyme/water mixture, yields the hydration water spectrum which is compared to the INS spectra of different kinds of ice in order to determine the changes induced by lysozyme on the hydrogen-bonded network of water. An additional comparison is performed by using a double-difference spectrum obtained by subtracting both the dry lysozyme and the trehalose spectra from the lysozyme/trehalose/water ternary spectrum. The effects of the mutual interactions among the three components, i.e. protein, disaccharide and water, are determined by comparison of the spectra of the dry systems (lysozyme, trehalose) with the difference spectra obtained from subtraction of the dry systems from the binary systems. It is concluded that the interfacial water more strongly affects the intermolecular mode region at low frequencies, whereas the vibrational spectra at high frequencies are more influenced by lysozyme and trehalose. |
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| Keywords: | Proteins Glass-forming disaccharides Ices Interfacial water Hydrogen-bonded network Inelastic neutron scattering |
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