Next Article in Journal
Theoretical Investigation on the Hydrogen Evolution, Oxygen Evolution, and Oxygen Reduction Reactions Performances of Two-Dimensional Metal-Organic Frameworks Fe3(C2X)12 (X = NH, O, S)
Previous Article in Journal
Yields of Photo-Proton Reactions on Nuclei of Nickel and Separation of Cobalt Isotopes from Irradiated Targets
 
 
Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
Journals
Molecules
Volume 27
Issue 5
10.3390/molecules27051526
molecules-logo
Submit to this Journal Review for this Journal Propose a Special Issue
► Article Menu

Article Menu

share Share announcement Help format_quote Cite question_answer Discuss in SciProfiles
first_page
settings
Order Article Reprints
Font Type:
Arial Georgia Verdana
Font Size:
Aa Aa Aa
Line Spacing:
Column Width:
Background:
Article

Interactions between Human Serum Albumin and Sulfadimethoxine Determined Using Spectroscopy and Molecular Docking

by
Yuai Zhang
1,2,†,
Yiqing Cao
3,†,
Yan Li
3,* and
Xuemei Zhang
1,*
1
Department of Pharmacology, School of Pharmacy, Fudan University, Shanghai 201203, China
2
NanChang Bozekang Pharmaceutical Technology Co., Ltd., Nanchang 330000, China
3
Department of Pharmaceutical Analysis, School of Pharmacy, Fudan University, Shanghai 201203, China
*
Authors to whom correspondence should be addressed.
†
These authors contributed equally to this work.
Molecules 2022, 27(5), 1526; https://doi.org/10.3390/molecules27051526
Submission received: 20 January 2022 / Revised: 19 February 2022 / Accepted: 22 February 2022 / Published: 24 February 2022
Browse Figures
Versions Notes

Abstract

Sulfonamides are widely used antibiotics in agricultural production. However, the potential threat of these drugs to human health has increased global concern. Human serum albumin (HSA) is the main reservoir and transporter of exogenous small molecules in humans. In this study, the interaction between sulfadimethoxine (SMT) and human serum albumin (HSA) was studied using spectroscopy and computer simulation. Our results showed that the hydrogen bonding and van der Waals forces drove SMT to enter the binding site I of HSA spontaneously and resulted in the fluorescence quenching of HSA. The stability of the HSA–SMT complex decreased with an increase in temperature. The binding of SMT to HSA induced alterations in the secondary structure of HSA, where the content of α-helix decreased from 61.0% of the free state to 59.0% of the compound state. The π–π, π–σ, and π–alkyl interactions between HSA and SMT were found to play important roles in maintaining the stability of the complex.
Keywords: sulfadimethoxine; molecular docking; spectroscopy; human serum albumin sulfadimethoxine; molecular docking; spectroscopy; human serum albumin

Share and Cite

MDPI and ACS Style

Zhang, Y.; Cao, Y.; Li, Y.; Zhang, X. Interactions between Human Serum Albumin and Sulfadimethoxine Determined Using Spectroscopy and Molecular Docking. Molecules 2022, 27, 1526. https://doi.org/10.3390/molecules27051526

AMA Style

Zhang Y, Cao Y, Li Y, Zhang X. Interactions between Human Serum Albumin and Sulfadimethoxine Determined Using Spectroscopy and Molecular Docking. Molecules. 2022; 27(5):1526. https://doi.org/10.3390/molecules27051526

Chicago/Turabian Style

Zhang, Yuai, Yiqing Cao, Yan Li, and Xuemei Zhang. 2022. "Interactions between Human Serum Albumin and Sulfadimethoxine Determined Using Spectroscopy and Molecular Docking" Molecules 27, no. 5: 1526. https://doi.org/10.3390/molecules27051526

APA Style

Zhang, Y., Cao, Y., Li, Y., & Zhang, X. (2022). Interactions between Human Serum Albumin and Sulfadimethoxine Determined Using Spectroscopy and Molecular Docking. Molecules, 27(5), 1526. https://doi.org/10.3390/molecules27051526

Article Metrics

Back to TopTop