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    Strong Hydration at the Poly(ethylene glycol) Brush/Albumin Solution Interface

    Year: 2020

    Journal: Langmuir, Volume 36, MAR 3, page 2030–2036

    Authors: Zhang, Kexin; Huang, Hao; Hung, Hsiang-Chieh; Leng, Chuan; Wei, Shuai; Crisci, Ralph; Jiang, Shaoyi; Chen, Zhan

    Organizations: Office of Naval ResearchOffice of Naval Research [N00014-16-1-3115, N00014-19-1-2171, N00014-16-1-3084]

    Albumin molecules are extensively used as biocompatible coatings, and poly(ethylene glycol) (PEG) materials are widely used for antifouling. PEG materials have excellent antifouling property because of their strong surface hydration. Our previous research indicates that hydration at the PEG/bovine serum albumin solution interface is stronger than that at the PEG/water interface. This research shows that this observation is general for different types of albumin molecules. Different albumins including bovine, porcine, rat, rabbit, and sheep serum albumins were studied in this research. It was found that the hydration at the PEG methacrylate (pOEGMA)/albumin solution interface is always stronger than that at the pOEGMA/water interface. Here, we define "strong interfacial hydration" as "ordered strongly hydrogen-bonded interfacial water". We believe that such a strong hydration is because of the strong hydration on the albumin surface, leading to its biocompatible property. All of the albumin molecules demonstrated stronger hydration on the pOEGMA surface compared to other protein molecules such as lysozyme and fibrinogen. The strong hydration on albumin molecules is related to the high surface coverage of glutamic acid and lysine with similar amounts.
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