A biophysical study on the mechanism of interactions of DOX or PTX with α-lactalbumin as a delivery carrier
Delavari, B
Mamashli, F
Bigdeli, B
Poursoleiman, A
Karami, L
Zolmajd-Haghighi, Z
Ghasemi, A
Samaei-Daryan, S
Hosseini, M
Haertlé, T
Muronetz, VI
Halskau, Ø
Moosavi-Movahedi, AA
Goliaei, B
Rezayan, AH
Saboury, AA
- Publication Type:
- Journal Article
- Citation:
- Scientific Reports, 2018, 8 (1)
- Issue Date:
- 2018-12-01
Open Access
Copyright Clearance Process
- Recently Added
- In Progress
- Open Access
This item is open access.
Full metadata record
Field | Value | Language |
---|---|---|
dc.contributor.author | Delavari, B | en_US |
dc.contributor.author | Mamashli, F | en_US |
dc.contributor.author | Bigdeli, B | en_US |
dc.contributor.author | Poursoleiman, A | en_US |
dc.contributor.author | Karami, L | en_US |
dc.contributor.author | Zolmajd-Haghighi, Z | en_US |
dc.contributor.author | Ghasemi, A | en_US |
dc.contributor.author | Samaei-Daryan, S | en_US |
dc.contributor.author | Hosseini, M | en_US |
dc.contributor.author | Haertlé, T | en_US |
dc.contributor.author | Muronetz, VI | en_US |
dc.contributor.author | Halskau, Ø | en_US |
dc.contributor.author | Moosavi-Movahedi, AA | en_US |
dc.contributor.author | Goliaei, B | en_US |
dc.contributor.author | Rezayan, AH | en_US |
dc.contributor.author | Saboury, AA | en_US |
dc.date.available | 2018-11-07 | en_US |
dc.date.issued | 2018-12-01 | en_US |
dc.identifier.citation | Scientific Reports, 2018, 8 (1) | en_US |
dc.identifier.uri | http://hdl.handle.net/10453/132654 | |
dc.description.abstract | © 2018, The Author(s). Doxorubicin and paclitaxel, two hydrophobic chemotherapeutic agents, are used in cancer therapies. Presence of hydrophobic patches and a flexible fold could probably make α-Lactalbumin a suitable carrier for hydrophobic drugs. In the present study, a variety of thermodynamic, spectroscopic, computational, and cellular techniques were applied to assess α-lactalbumin potential as a carrier for doxorubicin and paclitaxel. According to isothermal titration calorimetry data, the interaction between α-lactalbumin and doxorubicin or paclitaxel is spontaneous and the K (M−1) value for the interaction of α-lactalbumin and paclitaxel is higher than that for doxorubicin. Differential scanning calorimetry and anisotropy results indicated formation of α-lactalbumin complexes with doxorubicin or paclitaxel. Furthermore, molecular docking and dynamic studies revealed that TRPs are not involved in α-Lac’s interaction with Doxorubicin while TRP 60 interacts with paclitaxel. Based on Pace analysis to determine protein thermal stability, doxorubicin and paclitaxel induced higher and lower thermal stability in α-lactalbumin, respectively. Besides, fluorescence lifetime measurements reflected that the interaction between α-lactalbumin with doxorubicin or paclitaxel was of static nature. Therefore, the authors hypothesized that α-lactalbumin could serve as a carrier for doxorubicin and paclitaxel by reducing cytotoxicity and apoptosis which was demonstrated during our in vitro cell studies. | en_US |
dc.relation.ispartof | Scientific Reports | en_US |
dc.relation.isbasedon | 10.1038/s41598-018-35559-1 | en_US |
dc.subject.mesh | Calorimetry | en_US |
dc.subject.mesh | Calorimetry, Differential Scanning | en_US |
dc.subject.mesh | Cell Line, Tumor | en_US |
dc.subject.mesh | Cell Proliferation | en_US |
dc.subject.mesh | Circular Dichroism | en_US |
dc.subject.mesh | Doxorubicin | en_US |
dc.subject.mesh | Drug Carriers | en_US |
dc.subject.mesh | Drug Delivery Systems | en_US |
dc.subject.mesh | Drug Liberation | en_US |
dc.subject.mesh | Fluorescence Polarization | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Hydrogen Bonding | en_US |
dc.subject.mesh | Lactalbumin | en_US |
dc.subject.mesh | Molecular Docking Simulation | en_US |
dc.subject.mesh | Paclitaxel | en_US |
dc.subject.mesh | Protein Stability | en_US |
dc.subject.mesh | Thermodynamics | en_US |
dc.title | A biophysical study on the mechanism of interactions of DOX or PTX with α-lactalbumin as a delivery carrier | en_US |
dc.type | Journal Article | |
utslib.citation.volume | 1 | en_US |
utslib.citation.volume | 8 | en_US |
utslib.for | 0601 Biochemistry and Cell Biology | en_US |
pubs.embargo.period | Not known | en_US |
pubs.organisational-group | /University of Technology Sydney | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Engineering and Information Technology | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Engineering and Information Technology/School of Biomedical Engineering | |
utslib.copyright.status | open_access | |
pubs.issue | 1 | en_US |
pubs.publication-status | Published | en_US |
pubs.volume | 8 | en_US |
Abstract:
© 2018, The Author(s). Doxorubicin and paclitaxel, two hydrophobic chemotherapeutic agents, are used in cancer therapies. Presence of hydrophobic patches and a flexible fold could probably make α-Lactalbumin a suitable carrier for hydrophobic drugs. In the present study, a variety of thermodynamic, spectroscopic, computational, and cellular techniques were applied to assess α-lactalbumin potential as a carrier for doxorubicin and paclitaxel. According to isothermal titration calorimetry data, the interaction between α-lactalbumin and doxorubicin or paclitaxel is spontaneous and the K (M−1) value for the interaction of α-lactalbumin and paclitaxel is higher than that for doxorubicin. Differential scanning calorimetry and anisotropy results indicated formation of α-lactalbumin complexes with doxorubicin or paclitaxel. Furthermore, molecular docking and dynamic studies revealed that TRPs are not involved in α-Lac’s interaction with Doxorubicin while TRP 60 interacts with paclitaxel. Based on Pace analysis to determine protein thermal stability, doxorubicin and paclitaxel induced higher and lower thermal stability in α-lactalbumin, respectively. Besides, fluorescence lifetime measurements reflected that the interaction between α-lactalbumin with doxorubicin or paclitaxel was of static nature. Therefore, the authors hypothesized that α-lactalbumin could serve as a carrier for doxorubicin and paclitaxel by reducing cytotoxicity and apoptosis which was demonstrated during our in vitro cell studies.
Please use this identifier to cite or link to this item:
Download statistics for the last 12 months
Not enough data to produce graph