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      MS for investigation of time-dependent protein adsorption on surfaces in complex biological samples


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          This study aims at developing a nondestructive way for investigating protein adsorption on surfaces such as biomaterials using mass spectrometry.


          Ventricular cerebrospinal fluid in contact with poly carbonate membranes were used as adsorption templates and on-surface enzymatic digestion was applied to desorb proteins and cleave them into peptides. Mass spectrometric analysis provided both protein identification and determination of protein specific adsorption behavior.


          In general, the adsorption increased with incubation time but also protein-specific time-resolved adsorption patterns from the complex protein solution were discovered.


          The method developed is a promising tool for the characterization of biofouling, which sometimes causes rejection and encapsulation of implants and can be used as complement to other surface analytical techniques.


          One problem associated with artificial materials in the body is that proteins in the body interact with the surface, which sometimes causes rejection of the implant. In this study, a method for investigating the time-dependent protein adsorption on a surface originating from a complex biological protein solution was developed. Compared with other surface analyses, this method can identify what proteins that adsorbs on the surface. In addition, determination of protein-specific adsorption behavior in relation to incubation was possible. Generally, more proteins adsorbed to the surface with increase in incubation time.

          Most cited references30

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          Understanding protein adsorption phenomena at solid surfaces.

          Protein adsorption at solid surfaces plays a key role in many natural processes and has therefore promoted a widespread interest in many research areas. Despite considerable progress in this field there are still widely differing and even contradictive opinions on how to explain the frequently observed phenomena such as structural rearrangements, cooperative adsorption, overshooting adsorption kinetics, or protein aggregation. In this review recent achievements and new perspectives on protein adsorption processes are comprehensively discussed. The main focus is put on commonly postulated mechanistic aspects and their translation into mathematical concepts and model descriptions. Relevant experimental and computational strategies to practically approach the field of protein adsorption mechanisms and their impact on current successes are outlined. Copyright © 2011 Elsevier B.V. All rights reserved.
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            Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present.

            Mass-spectrometry-based proteomics is continuing to make major contributions to the discovery of fundamental biological processes and, more recently, has also developed into an assay platform capable of measuring hundreds to thousands of proteins in any biological system. The field has progressed at an amazing rate over the past five years in terms of technology as well as the breadth and depth of applications in all areas of the life sciences. Some of the technical approaches that were at an experimental stage back then are considered the gold standard today, and the community is learning to come to grips with the volume and complexity of the data generated. The revolution in DNA/RNA sequencing technology extends the reach of proteomic research to practically any species, and the notion that mass spectrometry has the potential to eventually retire the western blot is no longer in the realm of science fiction. In this review, we focus on the major technical and conceptual developments since 2007 and illustrate these by important recent applications.
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              Protein Interactions with Polymer Coatings and Biomaterials

              Protein adsorption is considered to be the most important factor of the interaction between polymeric biomaterials and body fluids or tissues. Water-mediated hydrophobic and hydration forces as well as electrostatic interactions are believed to be the major factors of protein adsorption. A systematic analysis of various monolayer systems has resulted in general guidelines, the so-called "Whitesides rules". These concepts have been successfully applied for designing various protein-resistant surfaces and are being studied to expand the understanding of protein-material interactions beyond existing limitations. Theories on the mechanisms of protein adsorption are constantly being improved due to the fast-developing analytical technologies. This Review is aimed at improving these empirical guidelines with regard to present theoretical and analytical advances. Current analytical methods to test mechanistic hypotheses and theories of protein-surface interactions will be discussed. Special focus will be given to state-of-the-art bioinert and biospecific coatings and their applications in biomedicine.

                Author and article information

                Future Sci OA
                Future Sci OA
                Future Science OA
                Future Science Ltd (London, UK )
                November 2015
                01 November 2015
                : 1
                : 4
                : FSO32
                [1 ]Department of Chemistry-BMC, Science for Life Laboratory, Uppsala University, PO Box 599, SE-751 24 Uppsala, Sweden
                [2 ]Department of Engineering Sciences, Uppsala University, PO Box 534, SE-751 21 Uppsala, Sweden
                Author notes
                *Author for correspondence: torgny.undin@ 123456gmail.com
                © T Undin

                This work is licensed under a Creative Commons Attribution 4.0 License

                Research Article

                ms,on-surface digestion,polycarbonate membrane,time-resolved protein adsorption,ventricular cerebrospinal fluid


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