Dominant albumin-surface interactions under independent control of surface charge and wettability

S. Guo , D. Pranantyo , E.-T. Kang , X. J. Loh , X. Zhu , Dominik Jańczewski , K.G. Neoh


Understanding protein adsorption behaviors on solid surfaces constitutes an important step toward development of efficacious and biocompatible medical devices. Both surface charge and wettability have been shown to influence protein adsorption attributes, including kinetics, quantities, deformation, and reversibility. However, determining the dominant interaction in these surface-induced phenomena is challenging because of the complexity of inter-related mechanisms at the liquid/solid interface. Herein, we reveal the dominant interfacial forces in these essential protein adsorption attributes under the influence of a combination of surface charge and wettability, using quartz crystal microbalance with dissipation monitoring and atomic force microscopy-based force spectroscopy on a series of model surfaces. These surfaces were fabricated via layer-by-layer assembly, which allowed two-dimensional control of surface charge and wettability with minimal cross-parameter dependency. We focused on a soft globular protein, bovine serum albumin (BSA), which is prone to conformational changes during adsorption. The information obtained from the two techniques shows that both surface charge and hydrophobicity can increase the protein–surface interaction forces and the adsorbed amount. However, surface hydrophobicity triggered a greater extent of deformation in the adsorbed BSA molecules, leading to more dehydration, spreading, and resistance to elution by ionic strength changes regardless of the surface charge. The role played by the surface charge in the adsorbed protein conformation and extent of desorption induced by changes in the ionic strength is secondary to that of surface hydrophobicity. These findings advance the understanding of how surface chemistry and properties can be tailored for directing protein–substrate interactions.
Author S. Guo
S. Guo,,
, D. Pranantyo
D. Pranantyo,,
, E.-T. Kang
E.-T. Kang,,
, X. J. Loh
X. J. Loh,,
, X. Zhu
X. Zhu,,
, Dominik Jańczewski (FC / LTP)
Dominik Jańczewski,,
- Laboratory Of Technological Processes
, K.G. Neoh
K.G. Neoh,,
Journal seriesLangmuir, ISSN 0743-7463
Issue year2018
Publication size in sheets0.65
Keywords in Englishlayer by layer, protein, BSA, adsorption
ASJC Classification1603 Electrochemistry; 1607 Spectroscopy; 2500 General Materials Science; 3104 Condensed Matter Physics; 3110 Surfaces and Interfaces
Abstract in Polishxxx
Languageen angielski
2018_Langmuir_GuoS.PDF 708.39 KB
Score (nominal)35
Score sourcejournalList
ScoreMinisterial score = 35.0, 26-06-2020, ArticleFromJournal
Publication indicators WoS Citations = 0; Scopus Citations = 6; Scopus SNIP (Source Normalised Impact per Paper): 2016 = 1.188; WoS Impact Factor: 2018 = 3.683 (2) - 2018=3.888 (5)
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