Spectroscopic evaluation of Zn (II) complexes with drug analogues: Interactions with BSA and the pH effect on the drug-Zn (II) system.
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| Title: | Spectroscopic evaluation of Zn (II) complexes with drug analogues: Interactions with BSA and the pH effect on the drug-Zn (II) system. |
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| Authors: | Vlasiou, Manolis C.1 (AUTHOR) vlasiou.m@unic.ac.cy, Pafiti, Kyriaki S.1 (AUTHOR) |
| Source: | Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy. Nov2020, Vol. 241, pN.PAG-N.PAG. 1p. |
| Subjects: | pH effect, Acetamide, Zinc ions, Zinc compounds, Carrier proteins, Amino acid residues, Fluorescence spectroscopy, Drug interactions |
| Abstract: | Using UV–Vis, FT-IR, fluorescence spectroscopy and protein-ligand docking, the interactions between the zinc complexes with drug analogues and bovine serum albumin were investigated. In addition, considering the ubiquitous presence of zinc ions in the human system, we studied the interactions between this ion with hymecromone, dihydropyridine analogue, and acetamide, as well as the pH influence on these systems. The complexes were synthesized by interaction between the ligands and the Zn (II) ion in a 2:1 M ratio. Elemental analysis, FT-IR, and UV–Vis spectroscopy studies investigated the structure of the synthesized complexes. Fluorescence spectroscopy, UV–Vis, molecular docking and molecular dynamics were used to study the interactions of the Zn complexes with the BSA. The drug-Zn (II) system's pH effect was investigated using UV–Vis spectroscopy. After the complexation with the zinc, the drug molecules exhibited higher apparent binding affinity to BSA. BSA's fluorescence efficiency by the drug analogues was enhanced. In addition, molecular modelling was used to classify the residue of amino acids in the BSA playing key roles in this binding interaction. An increase in pH appears to contribute to alkaline hydrolysis of the Zn (II) molecules. Unlabelled Image • Zinc metal ions contributes to different binding affinities of drugs on transport proteins. • Drug analogues can be vehicles for Zn and allies to its redox potential. • Zinc-drug complexes could be unstable to light alkaline conditions. [ABSTRACT FROM AUTHOR] |
| Copyright of Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 145233788 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Spectroscopic evaluation of Zn (II) complexes with drug analogues: Interactions with BSA and the pH effect on the drug-Zn (II) system. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Vlasiou%2C+Manolis+C%2E%22">Vlasiou, Manolis C.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> vlasiou.m@unic.ac.cy</i><br /><searchLink fieldCode="AR" term="%22Pafiti%2C+Kyriaki+S%2E%22">Pafiti, Kyriaki S.</searchLink><relatesTo>1</relatesTo> (AUTHOR) – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Spectrochimica+Acta+Part+A%3A+Molecular+%26+Biomolecular+Spectroscopy%22">Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy</searchLink>. Nov2020, Vol. 241, pN.PAG-N.PAG. 1p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22pH+effect%22">pH effect</searchLink><br /><searchLink fieldCode="DE" term="%22Acetamide%22">Acetamide</searchLink><br /><searchLink fieldCode="DE" term="%22Zinc+ions%22">Zinc ions</searchLink><br /><searchLink fieldCode="DE" term="%22Zinc+compounds%22">Zinc compounds</searchLink><br /><searchLink fieldCode="DE" term="%22Carrier+proteins%22">Carrier proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Amino+acid+residues%22">Amino acid residues</searchLink><br /><searchLink fieldCode="DE" term="%22Fluorescence+spectroscopy%22">Fluorescence spectroscopy</searchLink><br /><searchLink fieldCode="DE" term="%22Drug+interactions%22">Drug interactions</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Using UV–Vis, FT-IR, fluorescence spectroscopy and protein-ligand docking, the interactions between the zinc complexes with drug analogues and bovine serum albumin were investigated. In addition, considering the ubiquitous presence of zinc ions in the human system, we studied the interactions between this ion with hymecromone, dihydropyridine analogue, and acetamide, as well as the pH influence on these systems. The complexes were synthesized by interaction between the ligands and the Zn (II) ion in a 2:1 M ratio. Elemental analysis, FT-IR, and UV–Vis spectroscopy studies investigated the structure of the synthesized complexes. Fluorescence spectroscopy, UV–Vis, molecular docking and molecular dynamics were used to study the interactions of the Zn complexes with the BSA. The drug-Zn (II) system's pH effect was investigated using UV–Vis spectroscopy. After the complexation with the zinc, the drug molecules exhibited higher apparent binding affinity to BSA. BSA's fluorescence efficiency by the drug analogues was enhanced. In addition, molecular modelling was used to classify the residue of amino acids in the BSA playing key roles in this binding interaction. An increase in pH appears to contribute to alkaline hydrolysis of the Zn (II) molecules. Unlabelled Image • Zinc metal ions contributes to different binding affinities of drugs on transport proteins. • Drug analogues can be vehicles for Zn and allies to its redox potential. • Zinc-drug complexes could be unstable to light alkaline conditions. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.saa.2020.118641 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 1 StartPage: N.PAG Subjects: – SubjectFull: pH effect Type: general – SubjectFull: Acetamide Type: general – SubjectFull: Zinc ions Type: general – SubjectFull: Zinc compounds Type: general – SubjectFull: Carrier proteins Type: general – SubjectFull: Amino acid residues Type: general – SubjectFull: Fluorescence spectroscopy Type: general – SubjectFull: Drug interactions Type: general Titles: – TitleFull: Spectroscopic evaluation of Zn (II) complexes with drug analogues: Interactions with BSA and the pH effect on the drug-Zn (II) system. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Vlasiou, Manolis C. – PersonEntity: Name: NameFull: Pafiti, Kyriaki S. IsPartOfRelationships: – BibEntity: Dates: – D: 05 M: 11 Text: Nov2020 Type: published Y: 2020 Identifiers: – Type: issn-print Value: 13861425 Numbering: – Type: volume Value: 241 Titles: – TitleFull: Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy Type: main |
| ResultId | 1 |