Adsorption behaviour and surfactant elution of cationic salivary proteins at solid/liquid interfaces,studied by in situ ellipsometry |
| |
| Institution: | 1. Biomedical Laboratory Science, Faculty of Health and Society, Malmö University, SE-205 06 Malmö, Sweden;2. Prosthetic Dentistry, Faculty of Odontology, Malmö University, SE-205 06 Malmö, Sweden;1. Nagoya Institute of Technology, Gokiso cho, Showa ku, Nagoya 466-8555, Japan;2. ORTHOREBIRTH Co. Ltd., 3-17-43 Chigasaki-Higashi, Tsuzuki-ku, Yokohama 224-0033, Japan;1. KLK Oleo, SDN BHD, Menara KLK, Muliara Damansara, 47810 Petaling Jaya, Selanger, Malaysia;2. ISIS Facility, Rutherford Appleton Laboratory, STFC, Chilton, Didcot, OXON OX11 0QX, UK;3. Physical and Theoretical Chemistry Laboratory, Oxford University, South Parks Road, Oxford OX1 3QZ, UK;4. School of Pharmacy and Biomolecular Sciences, Liverpool John Moores University, Liverpool L3 3AF, UK;5. Lonza UK, GB-Blackley, Manchester, Lancs M9 8ES, UK;1. Institut des Matériaux Jean Rouxel (IMN) – UMR6502, Université de Nantes, CNRS, 2 rue de la Houssinière, BP 32229, 44322 Nantes Cedex 3, France;2. Sorbonne Université, Faculté des Sciences et Ingénierie, UMR CNRS, Laboratoire de Chimie Physique – Matière et Rayonnement, boîte courrier 1140, 4 place Jussieu F-75252 Paris Cedex 05, France;1. CNRS - LMD - Ecole Normale Supérieure de Paris, France;2. Chair of Elasticity, Moscow State University, Leninskiye Gory, 1, Moscow, 119991, Russia;3. Department of Mathematical and Statistical Sciences, University of Alberta, Edmonton, AB T6G 2G1, Canada;1. ISIS, STFC, Rutherford Appleton Laboratory, Chilton, Didcot, Oxon OX11 0QX, UK;2. Physical and Theoretical Chemistry Laboratory, Oxford University, South Parks Road, Oxford OX1 3QZ, UK |
| |
| Abstract: | Adsorption of the cationic salivary proteins lactoferrin, lactoperoxidase, lysozyme and histatin 5 to pure (hydrophilic) and methylated (hydrophobized) silica surfaces was investigated by in situ ellipsometry. Effects of concentration (≤10 μg ml−1, for lysozyme ≤200 μg ml−1) and dependence of surface wettability, as well as adsorption kinetics and elutability of adsorbed films by buffer and sodium dodecyl sulphate (SDS) solutions were investigated. Results showed that the amounts adsorbed decreased in the order lactoferrin ≥ lactoperoxidase > lysozyme ≥ histatin 5. On hydrophilic silica, the adsorption was most likely driven by electrostatic interactions, which resulted in adsorbed amounts of lactoferrin that indicated the formation of a monolayer with both side-on and end-on adsorbed molecules. For lactoperoxidase the adsorbed amounts were somewhat higher than an end-on monolayer, lysozyme adsorption showed amounts corresponding to a side-on monolayer, and histatin 5 displayed adsorbed amounts in the range of a side-on monolayer. On hydrophobized substrata, the adsorption was also mediated by hydrophobic interactions, which resulted in lower adsorbed amounts of lactoferrin and lactoperoxidase; closer to side-on monolayer coverage. For both lysozyme and histatin 5 the adsorbed amounts were the same as on the hydrophilic silica. The investigated proteins exhibited fast adsorption kinetics, and the initial kinetics indicated mass transport controlled behaviour at low concentrations on both types of substrates. Buffer rinsing and SDS elution indicated that the proteins in general were more tightly bound to the hydrophobized surface compared to hydrophilic silica. Overall, the surface activity of the investigated proteins implicates their importance in the salivary film formation. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
