Protein Cross-Linking and Oligomerization through Dityrosine Formation upon Exposure to Ozone

Autoren

Christopher J Kampf
Fobang Liu
Kathrin Reinmuth-Selzle
Thomas Berkemeier
Hannah Meusel
Manabu Shiraiwa
Ulrich Pöschl

DOI

10.1021/acs.est.5b02902

eISSN

1520-5851

ISSN

0013-936X

Ausgabe der Veröffentlichung

18

Zeitschrift

Environmental Science & Technology

Sprache

en

Online publication date

2015

Paginierung

10859 - 10866

Datum der Veröffentlichung

2015

Status

Published

Herausgeber

American Chemical Society (ACS)

Herausgeber URL

http://dx.doi.org/10.1021/acs.est.5b02902

Datum der Datenerfassung

2023

Titel

Protein Cross-Linking and Oligomerization through Dityrosine Formation upon Exposure to Ozone

Ausgabe der Zeitschrift

49

Datenquelle: Crossref

Abstract

Air pollution is a potential driver for the increasing prevalence of allergic disease, and post-translational modification by air pollutants can enhance the allergenic potential of proteins. Here, the kinetics and mechanism of protein oligomerization upon ozone (O3) exposure were studied in coated-wall flow tube experiments at environmentally relevant O3 concentrations, relative humidities and protein phase states (amorphous solid, semisolid, and liquid). We observed the formation of protein dimers, trimers, and higher oligomers, and attribute the cross-linking to the formation of covalent intermolecular dityrosine species. The oligomerization proceeds fast on the surface of protein films. In the bulk material, reaction rates are limited by diffusion depending on phase state and humidity. From the experimental data, we derive a chemical mechanism and rate equations for a kinetic multilayer model of surface and bulk reaction enabling the prediction of oligomer formation. Increasing levels of tropospheric O3 in the Anthropocene may promote the formation of protein oligomers with enhanced allergenicity and may thus contribute to the increasing prevalence of allergies.

Addresses

Institute of Inorganic and Analytical Chemistry, Johannes Gutenberg University Mainz , 55128 Mainz, Germany.

Autoren

Christopher J Kampf
Fobang Liu
Kathrin Reinmuth-Selzle
Thomas Berkemeier
Hannah Meusel
Manabu Shiraiwa
Ulrich Pöschl

DOI

10.1021/acs.est.5b02902

eISSN

1520-5851

Externe Identifier

PubMed Identifier: 26287571

Funding acknowledgements

Deutsche Forschungsgemeinschaft: KA 4008/1-1
China Scholarship Council:
Johannes Gutenberg-Universität Mainz:
Max-Planck-Gesellschaft:

Open access

false

ISSN

0013-936X

Ausgabe der Veröffentlichung

18

Zeitschrift

Environmental science & technology

Schlüsselwörter

Ozone
Tyrosine
Proteins
Serum Albumin, Bovine
Air Pollutants
Chromatography, Gel
Spectrometry, Fluorescence
Humidity
Air Pollution
Protein Processing, Post-Translational
Diffusion
Kinetics
Models, Chemical
Protein Multimerization

Sprache

eng

Medium

Print-Electronic

Online publication date

2015

Paginierung

10859 - 10866

Datum der Veröffentlichung

2015

Status

Published

Datum der Datenerfassung

2015

Titel

Protein Cross-Linking and Oligomerization through Dityrosine Formation upon Exposure to Ozone.

Sub types

Research Support, Non-U.S. Gov't
Journal Article

Ausgabe der Zeitschrift

49

Datenquelle: Europe PubMed Central

Abstract

Air pollution is a potential driver for the increasing prevalence of allergic disease, and post-translational modification by air pollutants can enhance the allergenic potential of proteins. Here, the kinetics and mechanism of protein oligomerization upon ozone (O3) exposure were studied in coated-wall flow tube experiments at environmentally relevant O3 concentrations, relative humidities and protein phase states (amorphous solid, semisolid, and liquid). We observed the formation of protein dimers, trimers, and higher oligomers, and attribute the cross-linking to the formation of covalent intermolecular dityrosine species. The oligomerization proceeds fast on the surface of protein films. In the bulk material, reaction rates are limited by diffusion depending on phase state and humidity. From the experimental data, we derive a chemical mechanism and rate equations for a kinetic multilayer model of surface and bulk reaction enabling the prediction of oligomer formation. Increasing levels of tropospheric O3 in the Anthropocene may promote the formation of protein oligomers with enhanced allergenicity and may thus contribute to the increasing prevalence of allergies.

Autoren

Christopher J Kampf
Fobang Liu
Kathrin Reinmuth-Selzle
Thomas Berkemeier
Hannah Meusel
Manabu Shiraiwa
Ulrich Pöschl

Autoren-URL

https://www.ncbi.nlm.nih.gov/pubmed/26287571

DOI

10.1021/acs.est.5b02902

eISSN

1520-5851

Ausgabe der Veröffentlichung

18

Zeitschrift

Environ Sci Technol

Schlüsselwörter

Air Pollutants
Air Pollution
Chromatography, Gel
Diffusion
Humidity
Kinetics
Models, Chemical
Ozone
Protein Multimerization
Protein Processing, Post-Translational
Proteins
Serum Albumin, Bovine
Spectrometry, Fluorescence
Tyrosine

Sprache

eng

Country

United States

Paginierung

10859 - 10866

Datum der Veröffentlichung

2015

Status

Published

Datum, an dem der Datensatz öffentlich gemacht wurde

2016

Titel

Protein Cross-Linking and Oligomerization through Dityrosine Formation upon Exposure to Ozone.

Sub types

Journal Article
Research Support, Non-U.S. Gov't

Ausgabe der Zeitschrift

49

Datenquelle: PubMed

Protein Cross-Linking and Oligomerization through Dityrosine Formation upon Exposure to Ozone

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