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Molecular interaction of fibrinogen with zeolite nanoparticles
Fibrinogen is one of the key proteins that participate in the protein corona composition of many types of nanoparticles (NPs), and its conformational changes are crucial for activation of immune systems. Recently, we demonstrated that the fibrinogen highly contributed in the protein corona compositi...
Autores principales: | , , , , , , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6367512/ https://www.ncbi.nlm.nih.gov/pubmed/30733474 http://dx.doi.org/10.1038/s41598-018-37621-4 |
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author | Derakhshankhah, Hossein Hosseini, Atiyeh Taghavi, Fereshteh Jafari, Samira Lotfabadi, Alireza Ejtehadi, Mohammad Reza Shahbazi, Sahba Fattahi, Ali Ghasemi, Atiyeh Barzegari, Ebrahim Evini, Mina Saboury, Ali Akbar Shahri, Seyed Mehdi Kamali Ghaemi, Behnaz Ng, Eng-Poh Awala, Hussein Omrani, Fatemeh Nabipour, Iraj Raoufi, Mohammad Dinarvand, Rassoul shahpasand, Koorosh Mintova, Svetlana Hajipour, Mohammad Javad Mahmoudi, Morteza |
author_facet | Derakhshankhah, Hossein Hosseini, Atiyeh Taghavi, Fereshteh Jafari, Samira Lotfabadi, Alireza Ejtehadi, Mohammad Reza Shahbazi, Sahba Fattahi, Ali Ghasemi, Atiyeh Barzegari, Ebrahim Evini, Mina Saboury, Ali Akbar Shahri, Seyed Mehdi Kamali Ghaemi, Behnaz Ng, Eng-Poh Awala, Hussein Omrani, Fatemeh Nabipour, Iraj Raoufi, Mohammad Dinarvand, Rassoul shahpasand, Koorosh Mintova, Svetlana Hajipour, Mohammad Javad Mahmoudi, Morteza |
author_sort | Derakhshankhah, Hossein |
collection | PubMed |
description | Fibrinogen is one of the key proteins that participate in the protein corona composition of many types of nanoparticles (NPs), and its conformational changes are crucial for activation of immune systems. Recently, we demonstrated that the fibrinogen highly contributed in the protein corona composition at the surface of zeolite nanoparticles. Therefore, understanding the interaction of fibrinogen with zeolite nanoparticles in more details could shed light of their safe applications in medicine. Thus, we probed the molecular interactions between fibrinogen and zeolite nanoparticles using both experimental and simulation approaches. The results indicated that fibrinogen has a strong and thermodynamically favorable interaction with zeolite nanoparticles in a non-cooperative manner. Additionally, fibrinogen experienced a substantial conformational change in the presence of zeolite nanoparticles through a concentration-dependent manner. Simulation results showed that both E- and D-domain of fibrinogen are bound to the EMT zeolite NPs via strong electrostatic interactions, and undergo structural changes leading to exposing normally buried sequences. D-domain has more contribution in this interaction and the C-terminus of γ chain (γ(377–394)), located in D-domain, showed the highest level of exposure compared to other sequences/residues. |
format | Online Article Text |
id | pubmed-6367512 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-63675122019-02-14 Molecular interaction of fibrinogen with zeolite nanoparticles Derakhshankhah, Hossein Hosseini, Atiyeh Taghavi, Fereshteh Jafari, Samira Lotfabadi, Alireza Ejtehadi, Mohammad Reza Shahbazi, Sahba Fattahi, Ali Ghasemi, Atiyeh Barzegari, Ebrahim Evini, Mina Saboury, Ali Akbar Shahri, Seyed Mehdi Kamali Ghaemi, Behnaz Ng, Eng-Poh Awala, Hussein Omrani, Fatemeh Nabipour, Iraj Raoufi, Mohammad Dinarvand, Rassoul shahpasand, Koorosh Mintova, Svetlana Hajipour, Mohammad Javad Mahmoudi, Morteza Sci Rep Article Fibrinogen is one of the key proteins that participate in the protein corona composition of many types of nanoparticles (NPs), and its conformational changes are crucial for activation of immune systems. Recently, we demonstrated that the fibrinogen highly contributed in the protein corona composition at the surface of zeolite nanoparticles. Therefore, understanding the interaction of fibrinogen with zeolite nanoparticles in more details could shed light of their safe applications in medicine. Thus, we probed the molecular interactions between fibrinogen and zeolite nanoparticles using both experimental and simulation approaches. The results indicated that fibrinogen has a strong and thermodynamically favorable interaction with zeolite nanoparticles in a non-cooperative manner. Additionally, fibrinogen experienced a substantial conformational change in the presence of zeolite nanoparticles through a concentration-dependent manner. Simulation results showed that both E- and D-domain of fibrinogen are bound to the EMT zeolite NPs via strong electrostatic interactions, and undergo structural changes leading to exposing normally buried sequences. D-domain has more contribution in this interaction and the C-terminus of γ chain (γ(377–394)), located in D-domain, showed the highest level of exposure compared to other sequences/residues. Nature Publishing Group UK 2019-02-07 /pmc/articles/PMC6367512/ /pubmed/30733474 http://dx.doi.org/10.1038/s41598-018-37621-4 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Derakhshankhah, Hossein Hosseini, Atiyeh Taghavi, Fereshteh Jafari, Samira Lotfabadi, Alireza Ejtehadi, Mohammad Reza Shahbazi, Sahba Fattahi, Ali Ghasemi, Atiyeh Barzegari, Ebrahim Evini, Mina Saboury, Ali Akbar Shahri, Seyed Mehdi Kamali Ghaemi, Behnaz Ng, Eng-Poh Awala, Hussein Omrani, Fatemeh Nabipour, Iraj Raoufi, Mohammad Dinarvand, Rassoul shahpasand, Koorosh Mintova, Svetlana Hajipour, Mohammad Javad Mahmoudi, Morteza Molecular interaction of fibrinogen with zeolite nanoparticles |
title | Molecular interaction of fibrinogen with zeolite nanoparticles |
title_full | Molecular interaction of fibrinogen with zeolite nanoparticles |
title_fullStr | Molecular interaction of fibrinogen with zeolite nanoparticles |
title_full_unstemmed | Molecular interaction of fibrinogen with zeolite nanoparticles |
title_short | Molecular interaction of fibrinogen with zeolite nanoparticles |
title_sort | molecular interaction of fibrinogen with zeolite nanoparticles |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6367512/ https://www.ncbi.nlm.nih.gov/pubmed/30733474 http://dx.doi.org/10.1038/s41598-018-37621-4 |
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