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New sandwich-type polymeric potassium-dicyanoargentate(I) complex: synthesis, characterization and enzymatic activity.

ABSTRACT: Coordination compounds containing dicyanoargentate(I) have remarkable biological potential due to their therapeutic antibacterial, antifungal, antibiofilm, and anticancer properties. In this study, a new dicyanoargentate(I)-based complex was synthesized and characterized by various procedures (elemental, thermal, FT-IR for complex) involving crystal analysis of the complex. In addition, the biological activity of this new compound on the acetylcholinesterase (AChE) enzyme, an important enzyme for the nervous system, was investigated. When the infrared (IR) spectrum of the complex is examined, the OH vibration peak resulting from H₂O molecules in the structure at 3948-3337 cm^-1 and at 2138 cm^-1, along with a CN peak coordinated to Ag, can be seen, indicating that the mass remaining in the thermal degradation of the complex at 1000 ? C is the weight corresponding to the metal mixture consisting of K+Ag (calc.: 68.06). The crystal method revealed that the complex has a sandwich-like, polymeric chemical structure with layers formed by K⁺ cations and [Ag(CN)₂H₂O]^- anions. Therefore, the AChE enzyme has potential therapeutic uses in improving ACh levels in brain cells, in reducing various side effects, and in improving cognitive impairment, especially in advanced Alzheimer's disease patients. In this study, the activity of this newly synthesized complex on AChE was also investigated. As a result of this research, [Ag(CN)₂(H₂O)K] had 0.0282 ± 0.010 ?M Ki values against AChE. The compound was therefore a good inhibitor for the AChE enzyme. This type of compound can be used for the development of novel anticholinesterase drugs.

SUBMITTER: Korkmaz N

PROVIDER: S-EPMC7751906 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature

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New sandwich-type polymeric potassium-dicyanoargentate(I) complex: synthesis, characterization and enzymatic activity.

Korkmaz Nesrin N

Turkish journal of chemistry 20200818 4

Coordination compounds containing dicyanoargentate(I) have remarkable biological potential due to their therapeutic antibacterial, antifungal, antibiofilm, and anticancer properties. In this study, a new dicyanoargentate(I)-based complex was synthesized and characterized by various procedures (elemental, thermal, FT-IR for complex) involving crystal analysis of the complex. In addition, the biological activity of this new compound on the acetylcholinesterase (AChE) enzyme, an important enzyme fo ...[more]

PMID: 33488216

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Project description:The mode of action of Deltalac-acetogenins, strong inhibitors of bovine heart mitochondrial complex I, is different from that of traditional inhibitors such as rotenone and piericidin A [Murai, M., et al. (2007) Biochemistry 46 , 6409-6416]. As further exploration of these unique inhibitors might provide new insights into the terminal electron transfer step of complex I, we drastically modified the structure of Deltalac-acetogenins and characterized their inhibitory action. In particular, on the basis of structural similarity between the bis-THF and the piperazine rings, we here synthesized a series of piperazine derivatives. Some of the derivatives exhibited very potent inhibition at nanomolar levels. The hydrophobicity of the side chains and their balance were important structural factors for the inhibition, as is the case for the original Deltalac-acetogenins. However, unlike in the case of the original Deltalac-acetogenins, (i) the presence of two hydroxy groups is not crucial for the activity, (ii) the level of superoxide production induced by the piperazines is relatively high, (iii) the inhibitory potency for the reverse electron transfer is remarkably weaker than that for the forward event, and (iv) the piperazines efficiently suppressed the specific binding of a photoaffinity probe of natural-type acetogenins ([ (125)I]TDA) to the ND1 subunit. We therefore conclude that the action mechanism of the piperazine series differs from that of the original Deltalac-acetogenins. The photoaffinity labeling study using a newly synthesized photoreactive piperazine ([ (125)I]AFP) revealed that this compound binds to the 49 kDa subunit and an unidentified subunit, not ND1, with a frequency of approximately 1:3. A variety of traditional complex I inhibitors as well as Deltalac-acetogenins suppressed the specific binding of [ (125)I]AFP to the subunits. The apparent competitive behavior of inhibitors that seem to bind to different sites may be due to structural changes at the binding site, rather than occupying the same site. The meaning of the occurrence of diverse inhibitors exhibiting different mechanisms of action is discussed in light of the functionality of the membrane arm of complex I.

Project description:BackgroundNon-histone protein acylation is increasingly recognized as an important posttranslational modification, but little is known as to the biochemical properties of protein serine acylating enzymes.Methodology/principal findingsWe here report that we have identified a metal-stimulated serine octanoyltransferase activity in microsomes from human erythroleukemic (HEL) cells. The HEL acylating enzyme was linear with respect to time and protein, exhibited a neutral pH optimum (stimulated by cobalt and zinc), and inhibited by chelating reagents. Hydroxylamine treatment removed most, but not all, of the attached radioactivity. A salt extract of microsomal membranes contained the major portion of enzyme activity, indicating that this acyltransferase is not an integral membrane protein. Sucrose density fractionation showed that the acyltransferase activity is concentrated in the endoplasmic reticulum. In competition experiments, the acyltransferase was well inhibited by activated forms of fatty acids containing at least eight to fourteen carbons, but not by acetyl CoA. The zinc-stimulated HEL acyltransferase did not octanoylate proenkephalin, proopiomelanocortin, His-tagged proghrelin, or proghrelin lacking the amino-terminal His-tag stub of Gly-Ala-Met. The peptides des-acyl ghrelin and ACTH were also not acylated; however, des-acyl ghrelin containing the N-terminal tripeptide Gly-Ala-Met was acylated. Mutagenesis studies indicated a requirement for serine five residues from the amino terminus, reminiscent of myristoyl transferase, but not of ghrelin acylation. However, recombinant myristoyl transferase could not recapitulate the hydroxylamine sensitivity, zinc-stimulation, nor EDTA inhibition obtained with HEL acyltransferase, properties preserved in the HEL cell enzyme purified through four sequential chromatographic steps.Conclusions/significanceIn conclusion, our data demonstrate the presence of a zinc-stimulated acyltransferase activity concentrated in the endoplasmic reticulum in HEL cells which is likely to contribute to medium-chain protein lipidation.

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New sandwich-type polymeric potassium-dicyanoargentate(I) complex: synthesis, characterization and enzymatic activity.

Publications

New sandwich-type polymeric potassium-dicyanoargentate(I) complex: synthesis, characterization and enzymatic activity.

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