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Updated: Apr 26, 2026

Monitoring Protein Adsorption with Solid-state Nanopores
Published on: December 2, 2011
Understanding the structural parameters of biocompatible nanoparticles dictating protein fouling
Carlos E de Castro1, Bruno Mattei, Karin A Riske
1Centro de Ciências Naturais e Humanas, Universidade Federal do ABC , Santo André, Brazil.
Abstract:
The development of nanocarriers for biomedical applications requires that these nanocarriers have special properties, including resistance to nonspecific protein adsorption. In this study, the fouling properties of PLA- and PCL-based block copolymer nanoparticles (NPs) have been evaluated by placing them in contact with model proteins. Block copolymer NPs were produced through the self-assembly of PEOm-b-PLAn and PEOm-b-PCLn. This procedure yielded nanosized objects with distinct structural features dependent on the length of the hydrophobic and hydrophilic blocks and the volume ratio. The protein adsorption events were examined in relation to size, chain length, surface curvature, and hydrophilic chain density. Fouling by BSA and lysozyme was considerably reduced as the length of the hydrophilic PEO-stabilizing shell increases. In contrast to the case of hydrophilic polymer-grafted planar surfaces, the current investigations suggest that the hydrophilic chain density did not markedly influence protein fouling. The protein adsorption took place at the outer surface of the NPs since neither BSA nor lysozyme was able to diffuse within the hydrophilic layer due to geometric restrictions. Protein binding is an exothermic process, and it is modulated mainly by polymer features. The secondary structures of BSA and lysozyme were not affected by the adhesion phenomena.
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