2019
DOI: 10.1016/j.jphotochem.2019.111871
|View full text |Cite
|
Sign up to set email alerts
|

Spectral and molecular modelling studies of sulfadoxine interaction with bovine serum albumin

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
8
0

Year Published

2019
2019
2024
2024

Publication Types

Select...
6
1

Relationship

0
7

Authors

Journals

citations
Cited by 20 publications
(8 citation statements)
references
References 44 publications
0
8
0
Order By: Relevance
“…BSA (4 µM) was titrated with various concentrations of cloxyquin (0, 1,5,10,15,20,25,30,40,60,70, and 80 µM) at different temperatures including 290, 300, and 310 K. The reactions were carried out in duplicate and its fluorescence spectra were detected in a range of 285-450 nm upon the excitation wavelength of 280 nm by using a QuantaMaster™ 40 spectrofluorometer (Photon Technology International, Inc., London, ON, Canada). The bandwidths of both excitation and emission units were set to be 1 nm.…”
Section: Steady-state Fluorescence Measurementmentioning
confidence: 99%
See 1 more Smart Citation
“…BSA (4 µM) was titrated with various concentrations of cloxyquin (0, 1,5,10,15,20,25,30,40,60,70, and 80 µM) at different temperatures including 290, 300, and 310 K. The reactions were carried out in duplicate and its fluorescence spectra were detected in a range of 285-450 nm upon the excitation wavelength of 280 nm by using a QuantaMaster™ 40 spectrofluorometer (Photon Technology International, Inc., London, ON, Canada). The bandwidths of both excitation and emission units were set to be 1 nm.…”
Section: Steady-state Fluorescence Measurementmentioning
confidence: 99%
“…Each domain can be categorized into two subdomains, namely A and B [14]. There are two tryptophan residues, Trp134 and Trp213 located in the subdomains IA and IIA of BSA, respectively [15], in which their intrinsic fluorescence is sensitive to microenvironmental changes [16] and widely employed as an inherent probe for investigation of BSA-drug interaction. There are three major binding pockets of drug that have been identified on the BSA structure and assigned as sites I, II, and III.…”
Section: Introductionmentioning
confidence: 99%
“…Fluorescence spectroscopy technology has good sensitivity to the inherent fluorescence of most proteins, [ 27 ] therefore it is commonly used to study the interaction of ligands with proteins. [ 28 ] Figure 1 is the fluorescence emission spectrum of the Try–CAPE, Pep–CAPE, and α ‐Chy–CAPE systems at 298.15 K. The amino acid residues of the proteases contain fluorescence, such as tryptophan (Trp) and tyrosine (Tyr) residues.…”
Section: Resultsmentioning
confidence: 99%
“…Fluorescence spectroscopy technology has good sensitivity to the inherent fluorescence of most proteins, [27] therefore it is commonly used to study the interaction of ligands with proteins. [28] the fluorescence intensity of the protease will decrease.…”
Section: Fluorescence Quenching Of Protease By Capementioning
confidence: 99%
“…This technique is very sensitive to changes in polarity of the protein fluorophores, being performed through the simultaneous measurement of excitation and emission wavelengths, under the condition of Δ λ = λ emission -λ excitation , with Δ λ = 60 nm for Trp residues andΔ λ= 15 nm for the study of Tyr residues(Bagalkoti et al, 2019). The synchronous fluorescence spectra for in Fig.5.…”
mentioning
confidence: 99%