Study on the fluorescence properties of the interaction between felodipine and bovine serum protein
The interaction between felodipine and bovine serum protein was studied, the optimal experimental conditions were selected, and the fluorescence quenching mechanism was discussed. The interaction between filodipine and bovine serum protein was determined by UV spectrophotometry, and the optimal expe...
Main Authors: | , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
EDP Sciences
2021-01-01
|
Series: | E3S Web of Conferences |
Subjects: | |
Online Access: | https://www.e3s-conferences.org/articles/e3sconf/pdf/2021/76/e3sconf_icepese2021_01023.pdf |
id |
doaj-e18558dd260f45ddbc8d0e9c3a1a3315 |
---|---|
record_format |
Article |
spelling |
doaj-e18558dd260f45ddbc8d0e9c3a1a33152021-08-09T08:02:26ZengEDP SciencesE3S Web of Conferences2267-12422021-01-013000102310.1051/e3sconf/202130001023e3sconf_icepese2021_01023Study on the fluorescence properties of the interaction between felodipine and bovine serum proteinLi Shuxian0Bu Jialuo1Liu Wenbin2Liu Cuijuan3Lv Yuguang4College of Pharmacy, Jiamusi UniversityCollege of Pharmacy, Jiamusi UniversitySchool of materials science and Engineering, Jiamusi UniversityCollege of Pharmacy, Jiamusi UniversityCollege of Pharmacy, Jiamusi UniversityThe interaction between felodipine and bovine serum protein was studied, the optimal experimental conditions were selected, and the fluorescence quenching mechanism was discussed. The interaction between filodipine and bovine serum protein was determined by UV spectrophotometry, and the optimal experimental conditions were selected by control variable method. The mechanism of fluorescence quenching in the system was explored by fluorescence spectrophotometry. The fluorescence intensity of the system between felodipine and bovine serum protein was the most obvious under the experimental conditions of buffer solution pH 7.4, felodipine concentration 8.0*10-4mol/L, reaction time 30min and 25°C. Static fluorescence quenching caused by the formation of complex compounds.https://www.e3s-conferences.org/articles/e3sconf/pdf/2021/76/e3sconf_icepese2021_01023.pdfbovineserumproteinfelodipinecomplexfluorescence properties study |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Li Shuxian Bu Jialuo Liu Wenbin Liu Cuijuan Lv Yuguang |
spellingShingle |
Li Shuxian Bu Jialuo Liu Wenbin Liu Cuijuan Lv Yuguang Study on the fluorescence properties of the interaction between felodipine and bovine serum protein E3S Web of Conferences bovineserumprotein felodipine complex fluorescence properties study |
author_facet |
Li Shuxian Bu Jialuo Liu Wenbin Liu Cuijuan Lv Yuguang |
author_sort |
Li Shuxian |
title |
Study on the fluorescence properties of the interaction between felodipine and bovine serum protein |
title_short |
Study on the fluorescence properties of the interaction between felodipine and bovine serum protein |
title_full |
Study on the fluorescence properties of the interaction between felodipine and bovine serum protein |
title_fullStr |
Study on the fluorescence properties of the interaction between felodipine and bovine serum protein |
title_full_unstemmed |
Study on the fluorescence properties of the interaction between felodipine and bovine serum protein |
title_sort |
study on the fluorescence properties of the interaction between felodipine and bovine serum protein |
publisher |
EDP Sciences |
series |
E3S Web of Conferences |
issn |
2267-1242 |
publishDate |
2021-01-01 |
description |
The interaction between felodipine and bovine serum protein was studied, the optimal experimental conditions were selected, and the fluorescence quenching mechanism was discussed. The interaction between filodipine and bovine serum protein was determined by UV spectrophotometry, and the optimal experimental conditions were selected by control variable method. The mechanism of fluorescence quenching in the system was explored by fluorescence spectrophotometry. The fluorescence intensity of the system between felodipine and bovine serum protein was the most obvious under the experimental conditions of buffer solution pH 7.4, felodipine concentration 8.0*10-4mol/L, reaction time 30min and 25°C. Static fluorescence quenching caused by the formation of complex compounds. |
topic |
bovineserumprotein felodipine complex fluorescence properties study |
url |
https://www.e3s-conferences.org/articles/e3sconf/pdf/2021/76/e3sconf_icepese2021_01023.pdf |
work_keys_str_mv |
AT lishuxian studyonthefluorescencepropertiesoftheinteractionbetweenfelodipineandbovineserumprotein AT bujialuo studyonthefluorescencepropertiesoftheinteractionbetweenfelodipineandbovineserumprotein AT liuwenbin studyonthefluorescencepropertiesoftheinteractionbetweenfelodipineandbovineserumprotein AT liucuijuan studyonthefluorescencepropertiesoftheinteractionbetweenfelodipineandbovineserumprotein AT lvyuguang studyonthefluorescencepropertiesoftheinteractionbetweenfelodipineandbovineserumprotein |
_version_ |
1721215030529097728 |