Abstract
Two-dimensional structures and characteristics of the complexes between sodium hyaluronate (NaHA) and bovine serum albumin (BSA) were studied by using a quartz crystal microbalance method and an atomic force microscope (AFM). NaHA did not adsorb on poly(γ-methyl-l-glutamate) (PMLG) film. On the other hand, the complexes adsorbed on it and the adsorption behaviors were found to be Langmuir types. With increasing weight ratio of BSA to NaHA, W BSA, the adsorption constants K decreased and the saturated adsorption masses Γ∞ increased. The adsorbed complexes were spherical particles and at saturated adsorption states they covered compactly on the PMLG film. The mean diameters d AFM estimated from the topographic images decreased from 70 to 54 nm with increasing W BSA. The adhesion force F ad and the frictional force F f between the complex layers and the AFM tip were obtained by using the contact mode of the AFM. With increasing W BSA, the values of F ad decreased and the values of F f increased. Compared with the frictional coefficient of the NaHA adsorption layer on the BSA monolayer, the values for the NaHA–BSA complex layer were found to be much higher.
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Acknowledgements
This research was supported by a grant from the Japan Society for the Promotion of Science (no. P 02183) and the Japan Health Sciences Foundation. Our thanks are extended to Seikagaku Kogyo Co. for supplying NaHA samples.
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Xu, S., Song, Y., Sato, S. et al. Surface structures of adsorption layers of sodium hyaluronate and bovine serum albumin complexes on poly(γ-methyl-l-glutamate) film and their surface properties. Colloid Polym Sci 283, 383–392 (2005). https://doi.org/10.1007/s00396-004-1157-5
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DOI: https://doi.org/10.1007/s00396-004-1157-5