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Current Organic Chemistry

Editor-in-Chief

ISSN (Print): 1385-2728
ISSN (Online): 1875-5348

Review Article

Control of Protein-Surface Interactions and Transport Properties: Functional Membranes and Operating Conditions

Author(s): Carla A.M. Portugal*

Volume 21, Issue 17, 2017

Page: [1725 - 1739] Pages: 15

DOI: 10.2174/1385272821666161228125325

Price: $65

Abstract

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 cell responses.

Keywords: Protein-surface interactions, protein structural changes, functional surfaces, stimuli-responsive membranes, membrane separation processes, biocatalysis, tissue engineering, biocompatibility.

Graphical Abstract

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