Mechanochemical synthesis of six Cu(II)complexes with selected thiols, their physicochemical characterization and interaction with DNA (Record no. 53528)

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fixed length control field 02562nam a2200289Ia 4500
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control field MX-MdCICY
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control field 20250625162430.0
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Transcribing agency CICY
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Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-19399
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Title Mechanochemical synthesis of six Cu(II)complexes with selected thiols, their physicochemical characterization and interaction with DNA
490 0# - SERIES STATEMENT
Volume/sequential designation Journal of Molecular Structure, 1265, p.133436, 2022
520 3# - SUMMARY, ETC.
Summary, etc. Cysteine together with histidine (His2Cys)has been identified as one of the ligands in Type 1 copper protein active sites, and Cu-S(Cys)interaction determines their unique spectroscopic features. This work reports the synthesis of model Cu(II)-thiolates, which could mimic the Type 1 sites. The Cu (II)-complexes with l-cysteine, n-acetylcysteine, l-glutathione, l-penicillamine, mercaptosuccinic acid and dl-dithiothreitol were synthesized by solvent-free mechanochemical methods. The complexes were found to be of the ML2 type as revealed by solid-state analytical techniques including FT-IR (ATR)spectroscopy, Raman spectroscopy, electronic absorption spectroscopy (diffuse reflectance), powder X-ray diffraction and desorption electrospray ionization mass spectrometry. These compounds are difficult, in some cases impossible, to isolate from solution because of rapid oxidation of thiols to disulfides and reduction of Cu(II)to Cu(I)or Cu(0). However, in the solid state these complexes were found to be highly stable and exhibited spectroscopic features similar to those in the Type 1 site. Interaction of the complexes with genomic DNA isolated from human blood was studied by electrophoresis, which showed that Cu(II)-mercaptosuccinic acid and Cu(II)-n-acetylcysteine caused extensive degradation, whereas Cu(II)-penicillamine amd Cu(II)-glutathione significantly degraded the DNA. Cu(II)-cysteine appears to form DNA adducts. Docking of Cu(II)-cysteine with thioredoxine reductase suggests that the complex has the potential to inhibit the activity of the enzyme.
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element CU(II)COMPLEXES
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element MECHANOCHEMICAL SYNTHESIS
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element TYPE 1 COPPER PROTEINS
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element DRUG-DNA INTERACTION
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Kazimi, S. G.
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Personal name Iqbal, M. S.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Mulligan, C. C.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Baseer, M.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Rehman, A. U.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Farooqi, F.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Person, J. R
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/1voRRqi1usxcr2dAehRi5nwPpq9bY35eF/view?usp=drivesdk">https://drive.google.com/file/d/1voRRqi1usxcr2dAehRi5nwPpq9bY35eF/view?usp=drivesdk</a>
Public note Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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Source of classification or shelving scheme Clasificación local
Koha item type Documentos solicitados
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-19399 25.06.2025 25.06.2025 Documentos solicitados