TY - JOUR
T1 - One-step antifouling coating of polystyrene using engineered polypeptides
AU - Zheng, Chuanbao
AU - Hussain, Zohaib
AU - Chen, Chang
AU - de Haas, Robbert Jan
AU - Deshpande, Siddharth
AU - Zhang, Zhisen
AU - Zuilhof, Han
AU - de Vries, Renko
PY - 2025/5
Y1 - 2025/5
N2 - Unwanted nonspecific adsorption caused by biomolecules influences the lifetime of biomedical devices and the sensing performance of biosensors. Previously, we have designed B-M-E triblock proteins that rapidly assemble on inorganic surfaces (gold and silica) and render those surfaces antifouling. The B-M-E triblock proteins have a surface-binding domain B, a multimerization domain M and an antifouling domain E. Many biomedical technologies involve organic (polymeric) surfaces where B-M-E triblock proteins could potentially be used. In this study, we computationally and experimentally investigate the assembly of B-M-E triblock proteins on polystyrene (PS) surfaces, using PS-binding peptides as a surface-binding block B. We used atomic force microscopy, dynamic light scattering, fluorescence microscopy and quartz crystal microbalance to test the antifouling coating functionality. We found that, like for inorganic surfaces, the B-M-E proteins with PS-binding peptides as B block, form homogeneous monomolecular layers on PS surfaces with good stability against PBS washing. The adsorbed protein layer fully prevents adsorption of fluorescently labeled bovine serum albumin to PS microfluidic chips. Similarly, no significant fouling was observed using quartz crystal microbalance when 1 % (v/v) or 10 % (v/v) human serum were used as foulants.
AB - Unwanted nonspecific adsorption caused by biomolecules influences the lifetime of biomedical devices and the sensing performance of biosensors. Previously, we have designed B-M-E triblock proteins that rapidly assemble on inorganic surfaces (gold and silica) and render those surfaces antifouling. The B-M-E triblock proteins have a surface-binding domain B, a multimerization domain M and an antifouling domain E. Many biomedical technologies involve organic (polymeric) surfaces where B-M-E triblock proteins could potentially be used. In this study, we computationally and experimentally investigate the assembly of B-M-E triblock proteins on polystyrene (PS) surfaces, using PS-binding peptides as a surface-binding block B. We used atomic force microscopy, dynamic light scattering, fluorescence microscopy and quartz crystal microbalance to test the antifouling coating functionality. We found that, like for inorganic surfaces, the B-M-E proteins with PS-binding peptides as B block, form homogeneous monomolecular layers on PS surfaces with good stability against PBS washing. The adsorbed protein layer fully prevents adsorption of fluorescently labeled bovine serum albumin to PS microfluidic chips. Similarly, no significant fouling was observed using quartz crystal microbalance when 1 % (v/v) or 10 % (v/v) human serum were used as foulants.
KW - Antifouling
KW - Elastin-like polypeptides
KW - MD simulations
KW - Polystyrene surface
KW - Solid-binding peptides
U2 - 10.1016/j.jcis.2025.01.147
DO - 10.1016/j.jcis.2025.01.147
M3 - Article
AN - SCOPUS:85215442639
SN - 0021-9797
VL - 685
SP - 350
EP - 360
JO - Journal of Colloid and Interface Science
JF - Journal of Colloid and Interface Science
ER -