Study of the effect of Cal-Red on the secondary structure of human serum albumin by spectroscopic techniques

2007 ◽  
Vol 846 (1-3) ◽  
pp. 112-118 ◽  
Author(s):  
Lijun Dong ◽  
Xingguo Chen ◽  
Zhide Hu
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Spectroscopic Techniques

Interaction of human serum albumin with liposomes of saturated and unsaturated lipids with different phase transition temperatures: a spectroscopic investigation by membrane probe PRODAN

RSC Advances ◽  
2014 ◽  
Vol 4 (28) ◽  
pp. 14335-14347 ◽  
Author(s):  
Raina Thakur ◽  
Anupam Das ◽  
Anjan Chakraborty
Keyword(s):  
Phase Transition ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Spectroscopic Techniques ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Unsaturated Lipids ◽  
Membrane Probe ◽  
Phase Transition Temperatures

The interaction of human serum albumin (HSA) with liposomes made of saturated and unsaturated phosphocholines has been studied using circular dichroism (CD), steady state and time resolved fluorescence spectroscopic techniques.

The effect of Berberine on the secondary structure of human serum albumin

2005 ◽  
Vol 743 (1-3) ◽  
pp. 79-84 ◽  
Author(s):  
Ying Li ◽  
WenYing He ◽  
Jianniao Tian ◽  
Jianghong Tang ◽  
Zhide Hu ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum

Unravelling the interaction of glipizide with human serum albumin using various spectroscopic techniques and molecular dynamics studies

2020 ◽  
Vol 39 (1) ◽  
pp. 336-347 ◽  
Author(s):  
Razique Anwer ◽  
Khalid I. AlQumaizi ◽  
Shafiul Haque ◽  
Pallavi Somvanshi ◽  
Nazia Ahmad ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Spectroscopic Techniques

scholarly journals Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 359 ◽  
Author(s):  
Usoltsev ◽  
Sitnikova ◽  
Kajava ◽  
Uspenskaya
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Ftir Spectroscopy ◽  
Conformational Changes ◽  
Data Interpretation ◽  
Random Coil ◽  
Helical Conformation ◽  
Structure Changes

Human serum albumin (HSA) is the most abundant protein in blood plasma. HSA is involved in the transport of hormones, fatty acids, and some other compounds, maintenance of blood pH, osmotic pressure, and many other functions. Although this protein is well studied, data about its conformational changes upon different denaturation factors are fragmentary and sometimes contradictory. This is especially true for FTIR spectroscopy data interpretation. Here, the effect of various denaturing agents on the structural state of HSA by using FTIR spectroscopy in the aqueous solutions was systematically studied. Our data suggest that the second derivative deconvolution method provides the most consistent interpretation of the obtained IR spectra. The secondary structure changes of HSA were studied depending on the concentration of the denaturing agent during acid, alkaline, and thermal denaturation. In general, the denaturation of HSA in different conditions is accompanied by a decrease in α-helical conformation and an increase in random coil conformation and the intermolecular β-strands. Meantime, some variation in the conformational changes depending on the type of the denaturation agent were also observed. The increase of β-structural conformation suggests that HSA may form amyloid-like aggregates upon the denaturation.

Disulfide bond cleavage of human serum albumin and alterations of its secondary structure by cis-diamminedichloroplatinum(II)

1992 ◽  
Vol 85 (1-3) ◽  
pp. 39-44 ◽  
Author(s):  
Naoko Ohta ◽  
Toshihisa Yotsuyanagi ◽  
Danni Chen ◽  
Rikako Ono ◽  
Shigekazu Ito ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Disulfide Bond ◽  
Bond Cleavage

scholarly journals Interaction of the Fungicide Tebuconazole with Human Serum Albumin: A Preliminary Study

2018 ◽  
Vol 62 (2) ◽  
pp. 85-91 ◽  
Author(s):  
J. Staničová ◽  
K. Želonková ◽  
V. Verebová ◽  
B. Holečková ◽  
J. Dianovský
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Triazole Fungicides ◽  
Number Of Binding Sites ◽  
Preliminary Study ◽  
Protein Macromolecule

Abstract The interactions between the fungicide tebuconazole and human serum albumin were investigated using fluorescence and circular dichroism spectroscopies. The experimental results showed that the fluorescence quenching of the protein by the tebuconazole molecule was a result of the formation of a ligand-protein complex with a binding constant of 8.51×103 l.mol−1 and the number of binding sites in the macromolecule was close to 1. These findings demonstrated the fact that although the binding affinity of tebuconazole to the protein may be slight, it was very similar to other triazole fungicides. In addition, tebuconazole stabilized the α-helical secondary structure of the human serum albumin due to the increase of the α-content in the protein macromolecule.

scholarly journals Probing the toxic interactions between the reactive dye Drimaren Red and Human Serum Albumin

2021 ◽  
Author(s):  
Thais Meira Menezes ◽  
Caio Rodrigo Dias de Assis ◽  
Antonio Marinho da Silva Neto ◽  
Priscila Gubert ◽  
Marcos Gomes Ghislandi ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Textile Industry ◽  
Electrostatic Interactions ◽  
Reactive Dye ◽  
Biological Macromolecules ◽  
Spectroscopic Techniques ◽  
Binding Characteristics

Azo dyes like Drimaren Red CL-5B (DR, CI Reactive Red 241) represent a class of compounds extensively used in the textile industry and are extremely dangerous to the environment and human health. Therefore, understanding the binding characteristics between such substances and biological macromolecules is essential from a toxic-kinetic perspective. The molecular interaction between DR and Human Serum Albumin (HSA) was investigated through spectroscopic techniques and molecular docking approaches. The results indicate that DR quenches HSA fluorescence following a static mechanism (corroborated by UV-Vis studies) with a moderate interaction (Ka~105 M-1), guided by electrostatic interactions (DS> 0 and DH< 0). DR is 5.52 nm distant from fluorophore residue Trp-214 (according to FRET investigations), and the interaction is mainly related to Tyr residues (as revealed by synchronous fluorescence). The Ellman assay identified a decrease in the content of HSA free thiol. The results of the RLS demonstrate that there are HSA alterations, suggesting damage to the confirmation of the protein. Molecular docking suggests the binding site of DR was located in subdomain IIB HSA, corroborating the experimental properties. Finally, the results suggest a high potential for DR toxicity triggered by contact with key proteins, which affects the biomolecule functionalities.

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