Records |
Author |
Attri, P.; Han, J.; Choi, S.; Choi, E.H.; Bogaerts, A.; Lee, W. |
Title |
CAP modifies the structure of a model protein from thermophilic bacteria: mechanisms of CAP-mediated inactivation |
Type |
A1 Journal article |
Year |
2018 |
Publication |
Scientific reports |
Abbreviated Journal |
Sci Rep-Uk |
Volume |
8 |
Issue |
1 |
Pages |
10218 |
Keywords |
A1 Journal article; Engineering sciences. Technology; Plasma Lab for Applications in Sustainability and Medicine – Antwerp (PLASMANT) |
Abstract |
Cold atmospheric plasma (CAP) has great potential for sterilization in the food industry, by deactivation of thermophilic bacteria, but the underlying mechanisms are largely unknown. Therefore, we investigate here whether CAP is able to denature/modify protein from thermophilic bacteria. We focus on MTH1880 (MTH) from Methanobacterium thermoautotrophicum as model protein, which we treated with dielectric barrier discharge (DBD) plasma operating in air for 10, 15 and 20 mins. We analysed the structural changes of MTH using circular dichroism, fluorescence and NMR spectroscopy, as well as the thermal and chemical denaturation, upon CAP treatment. Additionally, we performed molecular dynamics (MD) simulations to determine the stability, flexibility and solvent accessible surface area (SASA) of both the native and oxidised protein. |
Address |
|
Corporate Author |
|
Thesis |
|
Publisher |
|
Place of Publication |
|
Editor |
|
Language ![sorted by Language field, ascending order (up)](img/sort_asc.gif) |
|
Wos |
000437414500004 |
Publication Date |
2018-06-29 |
Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
Series Volume |
|
Series Issue |
|
Edition |
|
ISSN |
2045-2322 |
ISBN |
|
Additional Links |
UA library record; WoS full record; WoS citing articles |
Impact Factor |
4.259 |
Times cited |
6 |
Open Access |
OpenAccess |
Notes |
We gratefully acknowledge the European Marie Skłodowska-Curie Individual Fellowship “Anticancer-PAM” within Horizon2020 (grant number 743546). This work was also supported by NRF-2017R1A2B2008483 to W.L. through the National Research Foundation of Korea (NRF) and BK+ program (J.H.). E.H.C. acknowledges the NRF (NRF-2016K1A4A3914113 and No. 20100027963). The computational work was carried out using the Turing HPC infrastructure at the CalcUA core facility of the Universiteit Antwerpen (UA), a division of the Flemish Supercomputer Center VSC, funded by the Hercules Foundation, the Flemish Government (department EWI) and the UA. |
Approved |
Most recent IF: 4.259 |
Call Number |
PLASMANT @ plasmant @c:irua:152817c:irua:152431 |
Serial |
5002 |
Permanent link to this record |
|
|
|
Author |
Han, I.; Song, I.S.; Choi, S.A.; Lee, T.; Yusupov, M.; Shaw, P.; Bogaerts, A.; Choi, E.H.; Ryu, J.J. |
Title |
Bioactive Nonthermal Biocompatible Plasma Enhances Migration on Human Gingival Fibroblasts |
Type |
A1 Journal article |
Year |
2023 |
Publication |
Advanced healthcare materials |
Abbreviated Journal |
|
Volume |
12 |
Issue |
4 |
Pages |
2200527 |
Keywords |
A1 Journal article; Engineering sciences. Technology; Plasma Lab for Applications in Sustainability and Medicine – Antwerp (PLASMANT) |
Abstract |
This study hypothesizes that the application of low-dose nonthermal biocompatible dielectric barrier discharge plasma (DBD-NBP) to human gingival fibroblasts (HGFs) will inhibit colony formation but not cell death and induce matrix metalloproteinase (MMP) expression, extracellular matrix (ECM) degradation, and subsequent cell migration, which can result in enhanced wound healing. HGFs treated with plasma for 3 min migrate to each other across the gap faster than those in the control and 5-min treatment groups on days 1 and 3. The plasma-treated HGFs show significantly high expression levels of the cell cycle arrest-related p21 gene and enhanced MMP activity. Focal adhesion kinase (FAK) mediated attenuation of wound healing or actin cytoskeleton rearrangement, and plasma-mediated reversal of this attenuation support the migratory effect of DBD-NBP. Further, this work performs computer simulations to investigate the effect of oxidation on the stability and conformation of the catalytic kinase domain (KD) of FAK. It is found that the oxidation of highly reactive amino acids (AAs) Cys427, Met442, Cys559, Met571, Met617, and Met643 changes the conformation and increases the structural flexibility of the FAK protein and thus modulates its function and activity. Low-dose DBD-NBP-induces host cell cycle arrest, ECM breakdown, and subsequent migration, thus contributing to the enhanced wound healing process. |
Address |
|
Corporate Author |
|
Thesis |
|
Publisher |
|
Place of Publication |
|
Editor |
|
Language ![sorted by Language field, ascending order (up)](img/sort_asc.gif) |
|
Wos |
000897762100001 |
Publication Date |
2022-11-14 |
Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
Series Volume |
|
Series Issue |
|
Edition |
|
ISSN |
2192-2640 |
ISBN |
|
Additional Links |
UA library record; WoS full record; WoS citing articles |
Impact Factor |
10 |
Times cited |
|
Open Access |
OpenAccess |
Notes |
National Research Foundation of Korea; Kementerian Pendidikan, 2020R1I1A1A01073071 2021R1A6A1A03038785 ; |
Approved |
Most recent IF: 10; 2023 IF: 5.11 |
Call Number |
PLASMANT @ plasmant @c:irua:192804 |
Serial |
7242 |
Permanent link to this record |