Background: Proteins are important players in most membrane bioprocesses due to their high propensity
to interact with solid surfaces. Their structural behavior when adsorbing to surfaces is not only dependent
on protein structural stability, but also it is influenced by the chemical and topographical characteristics of
the surfaces. The intensity of protein-surface interactions has a determinant role in the transport of proteins
through porous media, thus influencing the performance of membrane and chromatographic separation processes.
Also, protein structural dynamics is intimately related to its molecular recognition ability, i.e. their capacity
to bind their specific substrates when used as an immobilized ligand or catalyst, to promote cell anchorage
to tissue scaffolds while mediators of cell-surface interactions in tissue engineering applications or to be
bound/recognized by specific ligands when they are the target solutes.
Objective: All these aspects motivated the development of several approaches envisaging a good control of
protein-surface interactions and the optimization of membrane processes. The design of functional surfaces capable
of an non-invasive modulation of the protein structural dynamics at surfaces and their binding ability has
been regarded as a key issue for the optimization of protein purification processes and for development of biomedical
devices, e.g. tissue scaffolds or implants, with improved biocompatibility and able to induce the desirable
Keywords: Protein-surface interactions, protein structural changes, functional surfaces, stimuli-responsive membranes, membrane separation
processes, biocatalysis, tissue engineering, biocompatibility.
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