Characterization of the Interaction of 6-Thioguanine with Human Serum Albumin by Surface-Enhanced Raman Scattering and Molecular Modeling

Li, Panfang; Gu, Hui; Zhang, Juling

doi:10.1080/00032719.2015.1017766

Cited by 8 publications

(4 citation statements)

References 42 publications

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“…Herein, the proposed Au NBP@Ag@hyaluronic acid microgels can play a role in the detection of 6-TG in human serum directly without any pretreatment for removing the biomacromolecules. According to the plasma concentration of 6-TG, Au NBP@Ag@hyaluronic acid microgels were applied to detect 6-TG quantitatively from 1.0 × 10 –7 to 1.0 × 10 –4 M by referencing the peak value at 916 cm –1 (N1–C6 bending vibration of purine ring) and 1294 cm –1 (N1–C6 stretching vibration of purine ring). , As shown in Figure A, the SERS intensity at 916 and 1297 cm –1 was strengthened gradually with the increase of 6-TG concentration and the intensity at 916 and 1297 cm –1 showed a linear correlation with the logarithm of 6-TG concentration in the range from 1.0 × 10 –7 to 1.0 × 10 –4 M, with the lowest detectable concentration of 1.0 × 10 –7 M. The corresponding standard equations were Y 916 = 186.7 X + 1509 and Y 1297 = 208.6 X + 1540 ( Y 916 was the intensity at 916 cm –1 , Y 1297 was the intensity at 1297 cm –1 , and X was the logarithm of 6-TG concentration), the correlation coefficient ( R 2 ) were 0.9646 and 0.9715, respectively (Figure B). Compared with other reported methods for the detection of 6-TG, the linear range of our proposed method was satisfactory (Table S1).…”

Section: Resultsmentioning

confidence: 99%

Oil-Free Gold Nanobipyramid@Ag Microgels as a Functional SERS Substrate for Direct Detection of Small Molecules in a Complex Sample Matrix

et al. 2021

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Surface-enhanced Raman scattering (SERS) is a supersensitive analysis technology based on the target molecular fingerprint information. The enhancement of local electromagnetic field of the SERS substrate would increase the target molecules' Raman intensity which adsorb on the surface of nanoparticles. However, the existing adhesive macromolecules in the complex mixed sample would interfere with the adsorption of small target molecules, and it weakens the Raman intensity of target molecules. Microgels are one of the potential materials to suppress the interference of adhesive macromolecules and to avoid the complex pretreatments. However, most of the current microgel synthesis methods involve complex operations with precise instrumentation or the interference of oil and organic reagents. In this work, a simple and oil-free method was proposed to synthesize the gold nanobipyramid (Au NBP) @Ag@hyaluronic acid microgel via the condensation reaction of carboxyl and amino groups. As a proof-of-concept demonstration for small-molecule detection, the rhodamine 6G (R6G) molecules were allowed to enter inside the microgel through the meshes and adsorb on the surface of Au NBP@Ag nanoparticles within 30 min, while the macromolecule (bovine serum albumin in this case) was retained outside the microgel in the meantime. In addition, under the combined action of lightning rod effect of Au NBP and surface plasmon resonance effect of silver render the microgels with high SERS activity. The synthetic Au NBP@Ag@hyaluronic acid microgels were applied to detect 6-thioguanine in the human serum without any pretreatment process, and it showed a high signal enhancement and stable SERS signal, which can satisfy the requirement of clinical diagnosis. These results show that the proposed microgels have potential applications in the field of point-of-care testing.

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Section: Resultsmentioning

confidence: 99%

Oil-Free Gold Nanobipyramid@Ag Microgels as a Functional SERS Substrate for Direct Detection of Small Molecules in a Complex Sample Matrix

et al. 2021

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“…So that the microenvironment of the Trp 214 is unaffected and mechanism of quenching ultimately unchanged. Therefore, 6-TG binds in the hydrophobic cavity of by static quenching mechanism (Li, Gu & Zhang 2015). As reported by An et al, 6-TG binds with subdomain IIA of HSA at same/near the warfarin binding site that was optimized by minimal energy using tripos force field with Gasteiger-Marsili charges ).…”

Section: Determination Of Binding Constant and Binding Stochiometrymentioning

confidence: 95%

Effect of guanidine hydrochloride and urea on the interaction of 6-thioguanine with human serum albumin: a spectroscopic and molecular dynamics based study

Ishtikhar

Khan

Chang

et al. 2016

Journal of Biomolecular Structure and Dynamics

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6-thioguanine (6-TG) is an antineoplastic, nucleobase guanine, purine analog drug belongs to thiopurine drug-family of antimetabolites. In the present study, we report an experimental approach towards interaction mechanism of 6-TG with human serum albumin (HSA) and examine the chemical stability of HSA in the presence of denaturants such as guanidine hydrochloride (GdnHCl) and urea. Interaction of 6-TG with HSA has been studied by various spectroscopic and spectropolarimeteric methods to investigate what short of binding occurs at physiological conditions. 6-TG binds in the hydrophobic cavity of subdomain IIA of HSA by static quenching mechanism which induces conformation alteration in the protein structure. That helpful for further study of denaturation process where change in secondary structures causes unfolding of protein that also responsible for severance of domain III from rest of the protein part. We have also performed molecular simulation and molecular docking study in the presence of denaturating agents to determine the binding property of 6-TG and the effect of denaturating agents on the structural activity of HSA. We had found that GdnHCl is more effective denaturating agent when compared to urea. Hence, this study provides straight evidence of the binding mechanism of 6-TG with HSA and the formation of intermediate or unfolding transition that causes unfolding of HSA.

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“…In the current study, to evaluate the interaction of TMP with HSA, we carried out the molecular docking process. Binding TMP to HSA and evaluating the interaction is important because the protein-ligand binding interaction can provide helpful knowledge about their structure as potential therapeutic agents [13]. In this study, selective sidechain residue flexibility is a valuable option provided by AutoDock Vina software [14].…”

Section: Molecular Docking and Molecular Dynamics Simulationmentioning

confidence: 99%

“…Among various properties of this protein, the main role of HSA is the transfer of various biological and drug molecules in the body to the target organs. Therefore, the interaction of the protein and different types of drugs has been explored in several studies because the interaction of drugs and HSA affects the structure of the drugs and their activity [12,13].…”

Section: Introductionmentioning

confidence: 99%

A Comprehensive Study of Human Serum Albumin Interaction With Trimethoprim Using Molecular Docking and Molecular Dynamics Methods: An Appropriate Tool for Drug Delivery Systems

Salehi

Shariatifar

Johkool

et al. 2021

The Journal of Qazvin University of Medical Sciences

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Background: Human serum albumin (HSA) is one of the most prominent protein in human blood. Trimethoprim (TMP) is an efficient antibiotic drug for treatment of pneumocystis pneumonia (PCP). Patients with HIV/AIDS and cancer are extremely affected by the disease due to immune system deficiency. Objective: The aim of this study is to evaluate the molecular dynamics simulation (MD) of HSA with TMP for drug delivery systems. Materials and methods: In the first step, the 3D structure of HSA and TMP were provided by PDB and PubChem respectively. Then, the molecular docking was done via AutoDock Vina software and the best complex was selected due to the lowest binding energy. Finally, the structural characteristics of the above complex was evaluated. Results: The results showed that TMP binds to the HSA molecule with a binding energy of -7.3 kcal/mol and this binding causes changes in third and second structure of the HSA. Thus, the RMSD and RG results proved the third structural changes and the results obtained from DSSP confirmed the second structural modifications. The TMP-HSA complex formation accompanied with hydrophobic interaction between residues; Tyr150 and Ala291, His288, Leu238, Leu219, Lys199, Lys195, Glu153 and TMP. The TMP molecule had two hydrogen bond with Arg222 residue and three with Ser192. Furthermore, the final PDB file of the MD simulation process showed that the TMP molecule had reaction HSA (IIA chain). Conclusion: Due to the extensive application of TMP in infectious disease and appropriate interaction with HSA, the complex could be used for targeted transport of nanoparticles in the future.

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Characterization of the Interaction of 6-Thioguanine with Human Serum Albumin by Surface-Enhanced Raman Scattering and Molecular Modeling

Cited by 8 publications

References 42 publications

Oil-Free Gold Nanobipyramid@Ag Microgels as a Functional SERS Substrate for Direct Detection of Small Molecules in a Complex Sample Matrix

Oil-Free Gold Nanobipyramid@Ag Microgels as a Functional SERS Substrate for Direct Detection of Small Molecules in a Complex Sample Matrix

Effect of guanidine hydrochloride and urea on the interaction of 6-thioguanine with human serum albumin: a spectroscopic and molecular dynamics based study

A Comprehensive Study of Human Serum Albumin Interaction With Trimethoprim Using Molecular Docking and Molecular Dynamics Methods: An Appropriate Tool for Drug Delivery Systems

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