Molecular interaction studies of initial electrostatic attraction between trypsin and the human PAR-2 receptor
Workers in livestock and fish cultivation are at increased risk of occupational airway damage caused by proteases. Proteases, such as trypsin, activate PAR-2 which in turn triggers an inflammatory response, potentially causing airway damage over time. There has been some speculation that PAR-2 recep...
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2020
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ftunivtroemsoe:oai:munin.uit.no:10037/18551 2023-05-15T18:06:10+02:00 Molecular interaction studies of initial electrostatic attraction between trypsin and the human PAR-2 receptor Kristoffersen, Tonje Håtveit 2020-01-16 https://hdl.handle.net/10037/18551 eng eng UiT Norges arktiske universitet UiT The Arctic University of Norway https://hdl.handle.net/10037/18551 openAccess Copyright 2020 The Author(s) VDP::Medisinske Fag: 700::Basale medisinske odontologiske og veterinærmedisinske fag: 710::Toksikologi: 730 VDP::Medical disciplines: 700::Basic medical dental and veterinary science disciplines: 710::Toxicology: 730 MBI-3911 Master thesis Mastergradsoppgave 2020 ftunivtroemsoe 2021-06-25T17:57:31Z Workers in livestock and fish cultivation are at increased risk of occupational airway damage caused by proteases. Proteases, such as trypsin, activate PAR-2 which in turn triggers an inflammatory response, potentially causing airway damage over time. There has been some speculation that PAR-2 receptors easier attract trypsin form species where this enzyme has a more negative electrostatic charge. A molecular modelling approach was used to assess the initial binding of the activating peptide segment of PAR-2 to trypsin from multiple animal species. Homology modelling was used to predict the structures of Pacific sardine trypsin, yellowtail trypsin and red king crab trypsin, as well as to construct the N-terminal peptide segment of PAR-2. Protein-protein docking was performed to predict initial surface interactions between the PAR-2 peptide segment and trypsin. The binding interaction was mapped, and the interacting amino acids were compared across the species, as well as the charge of the protein binding surfaces. The study indicates that there is, at least, a stronger initial interaction between the N-terminal peptide segment of PAR-2 and trypsin with a stronger negative charge. Master Thesis Red king crab University of Tromsø: Munin Open Research Archive Pacific |
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Open Polar |
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University of Tromsø: Munin Open Research Archive |
op_collection_id |
ftunivtroemsoe |
language |
English |
topic |
VDP::Medisinske Fag: 700::Basale medisinske odontologiske og veterinærmedisinske fag: 710::Toksikologi: 730 VDP::Medical disciplines: 700::Basic medical dental and veterinary science disciplines: 710::Toxicology: 730 MBI-3911 |
spellingShingle |
VDP::Medisinske Fag: 700::Basale medisinske odontologiske og veterinærmedisinske fag: 710::Toksikologi: 730 VDP::Medical disciplines: 700::Basic medical dental and veterinary science disciplines: 710::Toxicology: 730 MBI-3911 Kristoffersen, Tonje Håtveit Molecular interaction studies of initial electrostatic attraction between trypsin and the human PAR-2 receptor |
topic_facet |
VDP::Medisinske Fag: 700::Basale medisinske odontologiske og veterinærmedisinske fag: 710::Toksikologi: 730 VDP::Medical disciplines: 700::Basic medical dental and veterinary science disciplines: 710::Toxicology: 730 MBI-3911 |
description |
Workers in livestock and fish cultivation are at increased risk of occupational airway damage caused by proteases. Proteases, such as trypsin, activate PAR-2 which in turn triggers an inflammatory response, potentially causing airway damage over time. There has been some speculation that PAR-2 receptors easier attract trypsin form species where this enzyme has a more negative electrostatic charge. A molecular modelling approach was used to assess the initial binding of the activating peptide segment of PAR-2 to trypsin from multiple animal species. Homology modelling was used to predict the structures of Pacific sardine trypsin, yellowtail trypsin and red king crab trypsin, as well as to construct the N-terminal peptide segment of PAR-2. Protein-protein docking was performed to predict initial surface interactions between the PAR-2 peptide segment and trypsin. The binding interaction was mapped, and the interacting amino acids were compared across the species, as well as the charge of the protein binding surfaces. The study indicates that there is, at least, a stronger initial interaction between the N-terminal peptide segment of PAR-2 and trypsin with a stronger negative charge. |
format |
Master Thesis |
author |
Kristoffersen, Tonje Håtveit |
author_facet |
Kristoffersen, Tonje Håtveit |
author_sort |
Kristoffersen, Tonje Håtveit |
title |
Molecular interaction studies of initial electrostatic attraction between trypsin and the human PAR-2 receptor |
title_short |
Molecular interaction studies of initial electrostatic attraction between trypsin and the human PAR-2 receptor |
title_full |
Molecular interaction studies of initial electrostatic attraction between trypsin and the human PAR-2 receptor |
title_fullStr |
Molecular interaction studies of initial electrostatic attraction between trypsin and the human PAR-2 receptor |
title_full_unstemmed |
Molecular interaction studies of initial electrostatic attraction between trypsin and the human PAR-2 receptor |
title_sort |
molecular interaction studies of initial electrostatic attraction between trypsin and the human par-2 receptor |
publisher |
UiT Norges arktiske universitet |
publishDate |
2020 |
url |
https://hdl.handle.net/10037/18551 |
geographic |
Pacific |
geographic_facet |
Pacific |
genre |
Red king crab |
genre_facet |
Red king crab |
op_relation |
https://hdl.handle.net/10037/18551 |
op_rights |
openAccess Copyright 2020 The Author(s) |
_version_ |
1766177760737230848 |