Novel protein photocleavers: Chrysophanol and pachybasin
This study investigates the photocleavage activity of two anthraquinone derivatives isolated from T. harzianum ETS 323, chrysophanol and pachybasin, upon proteins. Pachybasin and chrysophanol exhibited different abilities to degrade BSA with UV 365 nm radiation. Between the two, pachybasin was shown...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2020-09-01
|
| Series: | Journal of Photochemistry and Photobiology |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2666469020300087 |
| _version_ | 1819140499684982784 |
|---|---|
| author | Kou-Cheng Peng Kun-Che Chang Shyue-Chu Ke JunRu Chen Shu-Ying Liu |
| author_facet | Kou-Cheng Peng Kun-Che Chang Shyue-Chu Ke JunRu Chen Shu-Ying Liu |
| author_sort | Kou-Cheng Peng |
| collection | DOAJ |
| description | This study investigates the photocleavage activity of two anthraquinone derivatives isolated from T. harzianum ETS 323, chrysophanol and pachybasin, upon proteins. Pachybasin and chrysophanol exhibited different abilities to degrade BSA with UV 365 nm radiation. Between the two, pachybasin was shown to be a better reagent in the degradation of proteins as exhibited on the SDS-PAGE. The action mode of these compounds to proteins was found to be random cleavage by an oxygen-derived radical. The resulting binding constants of chrysophanol to lysozyme and BSA were 6.9 ± 0.5 × 104 M−1 (ΔGo = −27.62 kJ/mol at 25°C) and 6.6 ± 0.4 × 105 M−1 (ΔGo = −33.22 kJ/mol), and of pachybasin to lysozyme and BSA were 5.0 ± 0.2 × 104 M−1 (ΔGo = −26.82 kJ/mol) and 1.1 ± 0.1 × 104 M−1(ΔGo = −23.07 kJ/mol), respectively. |
| first_indexed | 2024-12-22T11:39:32Z |
| format | Article |
| id | doaj.art-df4ac6cc34134c308cbb4ccd551e2589 |
| institution | Directory Open Access Journal |
| issn | 2666-4690 |
| language | English |
| last_indexed | 2024-12-22T11:39:32Z |
| publishDate | 2020-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Photochemistry and Photobiology |
| spelling | doaj.art-df4ac6cc34134c308cbb4ccd551e25892022-12-21T18:27:19ZengElsevierJournal of Photochemistry and Photobiology2666-46902020-09-013100008Novel protein photocleavers: Chrysophanol and pachybasinKou-Cheng Peng0Kun-Che Chang1Shyue-Chu Ke2JunRu Chen3Shu-Ying Liu4Department of Life Science, National Dong Hwa University, Hualien 974301, Taiwan, ROC.Department of Life Science, National Dong Hwa University, Hualien 974301, Taiwan, ROC.; Spencer Center for Vision Research, Byers Eye Institute, School of Medicine, Stanford University, Palo Alto, CA 94304, USADepartment of Physics, National Dong Hwa University, Hualien 974301, Taiwan, ROCDepartment of Physics, National Dong Hwa University, Hualien 974301, Taiwan, ROCDepartment of Biomedical Sciences, Da-Yeh University, Changhua 51591, Taiwan, ROC; Corresponding author.This study investigates the photocleavage activity of two anthraquinone derivatives isolated from T. harzianum ETS 323, chrysophanol and pachybasin, upon proteins. Pachybasin and chrysophanol exhibited different abilities to degrade BSA with UV 365 nm radiation. Between the two, pachybasin was shown to be a better reagent in the degradation of proteins as exhibited on the SDS-PAGE. The action mode of these compounds to proteins was found to be random cleavage by an oxygen-derived radical. The resulting binding constants of chrysophanol to lysozyme and BSA were 6.9 ± 0.5 × 104 M−1 (ΔGo = −27.62 kJ/mol at 25°C) and 6.6 ± 0.4 × 105 M−1 (ΔGo = −33.22 kJ/mol), and of pachybasin to lysozyme and BSA were 5.0 ± 0.2 × 104 M−1 (ΔGo = −26.82 kJ/mol) and 1.1 ± 0.1 × 104 M−1(ΔGo = −23.07 kJ/mol), respectively.http://www.sciencedirect.com/science/article/pii/S2666469020300087AnthraquinoneChrysophanolPachybasinProtein photocleaver |
| spellingShingle | Kou-Cheng Peng Kun-Che Chang Shyue-Chu Ke JunRu Chen Shu-Ying Liu Novel protein photocleavers: Chrysophanol and pachybasin Journal of Photochemistry and Photobiology Anthraquinone Chrysophanol Pachybasin Protein photocleaver |
| title | Novel protein photocleavers: Chrysophanol and pachybasin |
| title_full | Novel protein photocleavers: Chrysophanol and pachybasin |
| title_fullStr | Novel protein photocleavers: Chrysophanol and pachybasin |
| title_full_unstemmed | Novel protein photocleavers: Chrysophanol and pachybasin |
| title_short | Novel protein photocleavers: Chrysophanol and pachybasin |
| title_sort | novel protein photocleavers chrysophanol and pachybasin |
| topic | Anthraquinone Chrysophanol Pachybasin Protein photocleaver |
| url | http://www.sciencedirect.com/science/article/pii/S2666469020300087 |
| work_keys_str_mv | AT kouchengpeng novelproteinphotocleaverschrysophanolandpachybasin AT kunchechang novelproteinphotocleaverschrysophanolandpachybasin AT shyuechuke novelproteinphotocleaverschrysophanolandpachybasin AT junruchen novelproteinphotocleaverschrysophanolandpachybasin AT shuyingliu novelproteinphotocleaverschrysophanolandpachybasin |