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

AIM: This study aims at developing a nondestructive way for investigating protein adsorption on surfaces such as biomaterials using mass spectrometry. METHODS: Ventricular cerebrospinal fluid in contact with poly carbonate membranes were used as adsorption templates and on-surface enzymatic digestio...

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Autores principales: Undin, Torgny, Lind, Sara Bergström, Dahlin, Andreas P
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Future Science Ltd 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5137957/
https://www.ncbi.nlm.nih.gov/pubmed/28031905
http://dx.doi.org/10.4155/fso.15.32
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author Undin, Torgny
Lind, Sara Bergström
Dahlin, Andreas P
author_facet Undin, Torgny
Lind, Sara Bergström
Dahlin, Andreas P
author_sort Undin, Torgny
collection PubMed
description AIM: This study aims at developing a nondestructive way for investigating protein adsorption on surfaces such as biomaterials using mass spectrometry. METHODS: 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. RESULTS: In general, the adsorption increased with incubation time but also protein-specific time-resolved adsorption patterns from the complex protein solution were discovered. CONCLUSION: 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.
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spelling pubmed-51379572016-12-28 MS for investigation of time-dependent protein adsorption on surfaces in complex biological samples Undin, Torgny Lind, Sara Bergström Dahlin, Andreas P Future Sci OA Research Article AIM: This study aims at developing a nondestructive way for investigating protein adsorption on surfaces such as biomaterials using mass spectrometry. METHODS: 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. RESULTS: In general, the adsorption increased with incubation time but also protein-specific time-resolved adsorption patterns from the complex protein solution were discovered. CONCLUSION: 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. Future Science Ltd 2015-11-01 /pmc/articles/PMC5137957/ /pubmed/28031905 http://dx.doi.org/10.4155/fso.15.32 Text en © T Undin This work is licensed under a Creative Commons Attribution 4.0 License (http://creativecommons.org/licenses/by/4.0/)
spellingShingle Research Article
Undin, Torgny
Lind, Sara Bergström
Dahlin, Andreas P
MS for investigation of time-dependent protein adsorption on surfaces in complex biological samples
title MS for investigation of time-dependent protein adsorption on surfaces in complex biological samples
title_full MS for investigation of time-dependent protein adsorption on surfaces in complex biological samples
title_fullStr MS for investigation of time-dependent protein adsorption on surfaces in complex biological samples
title_full_unstemmed MS for investigation of time-dependent protein adsorption on surfaces in complex biological samples
title_short MS for investigation of time-dependent protein adsorption on surfaces in complex biological samples
title_sort ms for investigation of time-dependent protein adsorption on surfaces in complex biological samples
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5137957/
https://www.ncbi.nlm.nih.gov/pubmed/28031905
http://dx.doi.org/10.4155/fso.15.32
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