Studies of the Interaction between Isoimperatorin and Human Serum Albumin by Multispectroscopic Method: Identification of Possible Binding Site of the Compound Using Esterase Activity of the Protein
Isoimperatorin is one of the main components of Prangos ferulacea as a linear furanocoumarin and used as anti-inflammatory, analgesic, antispasmodic, and anticancer drug. Human serum albumin (HSA) is a principal extracellular protein with a high concentration in blood plasma and carrier for many dru...
Saved in:
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Wiley
2013-01-01
|
| Series: | The Scientific World Journal |
| Online Access: | http://dx.doi.org/10.1155/2013/305081 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1832556244543471616 |
|---|---|
| author | Samira Ranjbar Yalda Shokoohinia Sirous Ghobadi Nooshin Bijari Saeed Gholamzadeh Nastaran Moradi Mohammad Reza Ashrafi-Kooshk Abbas Aghaei Reza Khodarahmi |
| author_facet | Samira Ranjbar Yalda Shokoohinia Sirous Ghobadi Nooshin Bijari Saeed Gholamzadeh Nastaran Moradi Mohammad Reza Ashrafi-Kooshk Abbas Aghaei Reza Khodarahmi |
| author_sort | Samira Ranjbar |
| collection | DOAJ |
| description | Isoimperatorin is one of the main components of Prangos ferulacea as a linear furanocoumarin and used as anti-inflammatory, analgesic, antispasmodic, and anticancer drug. Human serum albumin (HSA) is a principal extracellular protein with a high concentration in blood plasma and carrier for many drugs to different molecular targets. Since the carrying of drug by HSA may affect on its structure and action, we decided to investigate the interaction between HSA and isoimperatorin using fluorescence and UV spectroscopy. Fluorescence data indicated that isoimperatorin quenches the intrinsic fluorescence of the HSA via a static mechanism and hydrophobic interaction play the major role in the drug binding. The binding average distance between isoimperatorin and Trp 214 of HSA was estimated on the basis of the theory of Förster energy transfer. Decrease of protein surface hydrophobicity (PSH) was also documented upon isoimperatorin binding. Furthermore, the synchronous fluorescence spectra show that the microenvironment of the tryptophan residues does not have obvious changes. Site marker compettive and fluorescence experiments revealed that the binding of isoimperatorin to HSA occurred at or near site I. Finally, the binding details between isoimperatorin and HSA were further confirmed by molecular docking and esterase activity inhibition studies which revealed that drug was bound at subdomain IIA. |
| format | Article |
| id | doaj-art-2ec7d8707b164f04acb0746e7088e5bc |
| institution | Kabale University |
| issn | 1537-744X |
| language | English |
| publishDate | 2013-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | The Scientific World Journal |
| spelling | doaj-art-2ec7d8707b164f04acb0746e7088e5bc2025-02-03T05:45:56ZengWileyThe Scientific World Journal1537-744X2013-01-01201310.1155/2013/305081305081Studies of the Interaction between Isoimperatorin and Human Serum Albumin by Multispectroscopic Method: Identification of Possible Binding Site of the Compound Using Esterase Activity of the ProteinSamira Ranjbar0Yalda Shokoohinia1Sirous Ghobadi2Nooshin Bijari3Saeed Gholamzadeh4Nastaran Moradi5Mohammad Reza Ashrafi-Kooshk6Abbas Aghaei7Reza Khodarahmi8Nano Drug Delivery Research Center, Kermanshah University of Medical Sciences, Kermanshah 6734667149, IranNovel Drug Delivery Research Center, School of Pharmacy, Kermanshah University of Medical Sciences, Kermanshah, IranDepartment of Biology, Faculty of Science, Razi University, Kermanshah, IranNano Drug Delivery Research Center, Kermanshah University of Medical Sciences, Kermanshah 6734667149, IranIsfahan Pharmaceutical Sciences Research Center, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, IranNano Drug Delivery Research Center, Kermanshah University of Medical Sciences, Kermanshah 6734667149, IranNano Drug Delivery Research Center, Kermanshah University of Medical Sciences, Kermanshah 6734667149, IranDepartment of Epidemiology, Kermanshah University of Medical Sciences, Kermanshah, IranNano Drug Delivery Research Center, Kermanshah University of Medical Sciences, Kermanshah 6734667149, IranIsoimperatorin is one of the main components of Prangos ferulacea as a linear furanocoumarin and used as anti-inflammatory, analgesic, antispasmodic, and anticancer drug. Human serum albumin (HSA) is a principal extracellular protein with a high concentration in blood plasma and carrier for many drugs to different molecular targets. Since the carrying of drug by HSA may affect on its structure and action, we decided to investigate the interaction between HSA and isoimperatorin using fluorescence and UV spectroscopy. Fluorescence data indicated that isoimperatorin quenches the intrinsic fluorescence of the HSA via a static mechanism and hydrophobic interaction play the major role in the drug binding. The binding average distance between isoimperatorin and Trp 214 of HSA was estimated on the basis of the theory of Förster energy transfer. Decrease of protein surface hydrophobicity (PSH) was also documented upon isoimperatorin binding. Furthermore, the synchronous fluorescence spectra show that the microenvironment of the tryptophan residues does not have obvious changes. Site marker compettive and fluorescence experiments revealed that the binding of isoimperatorin to HSA occurred at or near site I. Finally, the binding details between isoimperatorin and HSA were further confirmed by molecular docking and esterase activity inhibition studies which revealed that drug was bound at subdomain IIA.http://dx.doi.org/10.1155/2013/305081 |
| spellingShingle | Samira Ranjbar Yalda Shokoohinia Sirous Ghobadi Nooshin Bijari Saeed Gholamzadeh Nastaran Moradi Mohammad Reza Ashrafi-Kooshk Abbas Aghaei Reza Khodarahmi Studies of the Interaction between Isoimperatorin and Human Serum Albumin by Multispectroscopic Method: Identification of Possible Binding Site of the Compound Using Esterase Activity of the Protein The Scientific World Journal |
| title | Studies of the Interaction between Isoimperatorin and Human Serum Albumin by Multispectroscopic Method: Identification of Possible Binding Site of the Compound Using Esterase Activity of the Protein |
| title_full | Studies of the Interaction between Isoimperatorin and Human Serum Albumin by Multispectroscopic Method: Identification of Possible Binding Site of the Compound Using Esterase Activity of the Protein |
| title_fullStr | Studies of the Interaction between Isoimperatorin and Human Serum Albumin by Multispectroscopic Method: Identification of Possible Binding Site of the Compound Using Esterase Activity of the Protein |
| title_full_unstemmed | Studies of the Interaction between Isoimperatorin and Human Serum Albumin by Multispectroscopic Method: Identification of Possible Binding Site of the Compound Using Esterase Activity of the Protein |
| title_short | Studies of the Interaction between Isoimperatorin and Human Serum Albumin by Multispectroscopic Method: Identification of Possible Binding Site of the Compound Using Esterase Activity of the Protein |
| title_sort | studies of the interaction between isoimperatorin and human serum albumin by multispectroscopic method identification of possible binding site of the compound using esterase activity of the protein |
| url | http://dx.doi.org/10.1155/2013/305081 |
| work_keys_str_mv | AT samiraranjbar studiesoftheinteractionbetweenisoimperatorinandhumanserumalbuminbymultispectroscopicmethodidentificationofpossiblebindingsiteofthecompoundusingesteraseactivityoftheprotein AT yaldashokoohinia studiesoftheinteractionbetweenisoimperatorinandhumanserumalbuminbymultispectroscopicmethodidentificationofpossiblebindingsiteofthecompoundusingesteraseactivityoftheprotein AT sirousghobadi studiesoftheinteractionbetweenisoimperatorinandhumanserumalbuminbymultispectroscopicmethodidentificationofpossiblebindingsiteofthecompoundusingesteraseactivityoftheprotein AT nooshinbijari studiesoftheinteractionbetweenisoimperatorinandhumanserumalbuminbymultispectroscopicmethodidentificationofpossiblebindingsiteofthecompoundusingesteraseactivityoftheprotein AT saeedgholamzadeh studiesoftheinteractionbetweenisoimperatorinandhumanserumalbuminbymultispectroscopicmethodidentificationofpossiblebindingsiteofthecompoundusingesteraseactivityoftheprotein AT nastaranmoradi studiesoftheinteractionbetweenisoimperatorinandhumanserumalbuminbymultispectroscopicmethodidentificationofpossiblebindingsiteofthecompoundusingesteraseactivityoftheprotein AT mohammadrezaashrafikooshk studiesoftheinteractionbetweenisoimperatorinandhumanserumalbuminbymultispectroscopicmethodidentificationofpossiblebindingsiteofthecompoundusingesteraseactivityoftheprotein AT abbasaghaei studiesoftheinteractionbetweenisoimperatorinandhumanserumalbuminbymultispectroscopicmethodidentificationofpossiblebindingsiteofthecompoundusingesteraseactivityoftheprotein AT rezakhodarahmi studiesoftheinteractionbetweenisoimperatorinandhumanserumalbuminbymultispectroscopicmethodidentificationofpossiblebindingsiteofthecompoundusingesteraseactivityoftheprotein |