Synthesis of thiosulphonate and amino acid derivatives of benzochinone and predicted screening of their biological activity

Quinoid derivatives are attractive not only as interesting synthons for synthesis, but also as potential biologically active substances, so it is important to modify the compounds of the quinone series with different pharmacoform fragments. In this work, the structural design of chlorine and bromanyl disulfur-containing fragments, namely thiosulfonate, and chloranyl – a fragment of 4- aminobutanoic acid. Methods of synthesis were developed and physicochemical characteristics of thiosulfonate and amino acid derivatives were studied: 2,5-bis (thiosulfonate) -3,6-halogen -1,4- benzoquinones and 2,5-bis (3-carboxypropylamino) -3,6 - dichlorobenzoquinone. The prospects for the design of chlorine and bromanyl thiosulfonate fragments and chloranyl fragment of 4- aminobutanoic acid are confirmed by the results of predicting the biological activity of 5 a, b, 6 a, b, 7 using the online resource PASS Online. In particular, the substance 6a obtained by us is promising in terms of research on Antiviral (Picornavirus). The obtained results of predicted cytotoxicity screening indicate the feasibility of conducting experimental studies by in vitro methods on anticancer activity against cancer cell lines of hematopoietic and lymphoid tissue, lungs, skin, ovaries, blood, breast, kidney, colon, brain.

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Nigellothionins from Black Cumin (Nigella sativa L.) Seeds Demonstrate Strong Antifungal and Cytotoxic Activity

Antibiotics ◽

10.3390/antibiotics10020166 ◽

2021 ◽

Vol 10 (2) ◽

pp. 166

Author(s):

Anna S. Barashkova ◽

Vera S. Sadykova ◽

Victoria A. Salo ◽

Sergey K. Zavriev ◽

Eugene A. Rogozhin

Keyword(s):

Amino Acid ◽

Cytotoxic Activity ◽

Nigella Sativa ◽

Physicochemical Characteristics ◽

Amino Acid Sequences ◽

Biologically Active ◽

Stress Factors ◽

Clinical Isolates ◽

Black Cumin

High-cationic biologically active peptides of the thionins family were isolated from black cumin (Nigella sativa L.) seeds. According to their physicochemical characteristics, they were classified as representatives of the class I thionin subfamily. Novel peptides were called “Nigellothionins”, so-called because of their source plant. Thionins are described as components of plant innate immunity to environmental stress factors. Nine nigellothionins were identified in the plant in different amounts. Complete amino acid sequences were determined for three of them, and a high degree of similarity was detected. Three nigellothionins were examined for antifungal properties against collection strains. The dominant peptide, NsW2, was also examined for activity against clinical isolates of fungi. Cytotoxic activity was determined for NsW2. Nigellothionins activity against all collection strains and clinical isolates varied from absence to a value comparable to amphotericin B, which can be explained by the presence of amino acid substitutions in their sequences. Cytotoxic activity in vitro for NsW2 was detected at sub-micromolar concentrations. This has allowed us to propose an alteration of the molecular mechanism of action at different concentrations. The results obtained suggest that nigellothionins are natural compounds that can be used as antimycotic and anti-proliferative agents.

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In vitro anticancer potentiality and molecular modelling study of novel amino acid derivatives based on N1,N3-bis-(1-hydrazinyl-1-oxopropan-2-yl) isophthalamide

Journal of Enzyme Inhibition and Medicinal Chemistry ◽

10.1080/14756366.2019.1613390 ◽

2019 ◽

Vol 34 (1) ◽

pp. 1247-1258 ◽

Cited By ~ 3

Author(s):

Asmaa F. Kassem ◽

Gaber O. Moustafa ◽

Eman S. Nossier ◽

Hemat S. Khalaf ◽

Marwa M. Mounier ◽

...

Keyword(s):

Amino Acid ◽

Molecular Modelling ◽

Amino Acid Derivatives ◽

Modelling Study

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Novel Amino Acid Derivatives of Quinolines as Potential Antibacterial and Fluorophore Agents

Scientia Pharmaceutica ◽

10.3390/scipharm88040057 ◽

2020 ◽

Vol 88 (4) ◽

pp. 57

Author(s):

Oussama Moussaoui ◽

Rajendra Bhadane ◽

Riham Sghyar ◽

El Mestafa El Hadrami ◽

Soukaina El Amrani ◽

...

Keyword(s):

Amino Acid ◽

Methyl Esters ◽

Amino Acid Derivatives ◽

Bacterial Strains ◽

Fluorescent Properties ◽

Topoisomerase Iv ◽

Microdilution Method ◽

Hydrolysis Of ◽

Derivatives Of

A new series of amino acid derivatives of quinolines was synthesized through the hydrolysis of amino acid methyl esters of quinoline carboxamides with alkali hydroxide. The compounds were purified on silica gel by column chromatography and further characterized by TLC, NMR and ESI-TOF mass spectrometry. All compounds were screened for in vitro antimicrobial activity against different bacterial strains using the microdilution method. Most of the synthesized amino acid-quinolines show more potent or equipotent inhibitory action against the tested bacteria than their correspond esters. In addition, many of them exhibit fluorescent properties and could possibly be utilized as fluorophores. Molecular docking and simulation studies of the compounds at putative bacterial target enzymes suggest that the antimicrobial potency of these synthesized analogues could be due to enzyme inhibition via their favorable binding at the fluoroquinolone binding site at the GyrA subunit of DNA gyrase and/or the ParC subunit of topoisomerase-IV.

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Transforming growth factor alpha: mutation of aspartic acid 47 and leucine 48 results in different biological activities.

Molecular and Cellular Biology ◽

10.1128/mcb.8.3.1247 ◽

1988 ◽

Vol 8 (3) ◽

pp. 1247-1252 ◽

Cited By ~ 35

Author(s):

E Lazar ◽

S Watanabe ◽

S Dalton ◽

M B Sporn

Keyword(s):

Amino Acids ◽

Biological Activity ◽

Amino Acid ◽

Growth Factor ◽

Aspartic Acid ◽

Transforming Growth Factor ◽

Biologically Active ◽

Single Amino Acid ◽

Transforming Growth Factor Alpha ◽

Factor Alpha

To study the relationship between the primary structure of transforming growth factor alpha (TGF-alpha) and some of its functional properties (competition with epidermal growth factor (EGF) for binding to the EGF receptor and induction of anchorage-independent growth), we introduced single amino acid mutations into the sequence for the fully processed, 50-amino-acid human TGF-alpha. The wild-type and mutant proteins were expressed in a vector by using a yeast alpha mating pheromone promoter. Mutations of two amino acids that are conserved in the family of the EGF-like peptides and are located in the carboxy-terminal part of TGF-alpha resulted in different biological effects. When aspartic acid 47 was mutated to alanine or asparagine, biological activity was retained; in contrast, substitutions of this residue with serine or glutamic acid generated mutants with reduced binding and colony-forming capacities. When leucine 48 was mutated to alanine, a complete loss of binding and colony-forming abilities resulted; mutation of leucine 48 to isoleucine or methionine resulted in very low activities. Our data suggest that these two adjacent conserved amino acids in positions 47 and 48 play different roles in defining the structure and/or biological activity of TGF-alpha and that the carboxy terminus of TGF-alpha is involved in interactions with cellular TGF-alpha receptors. The side chain of leucine 48 appears to be crucial either indirectly in determining the biologically active conformation of TGF-alpha or directly in the molecular recognition of TGF-alpha by its receptor.

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“In vivo” amplification of biological activity of tetragastrin by amino acid hydroxamates

Bioscience Reports ◽

10.1007/bf01116693 ◽

1984 ◽

Vol 4 (12) ◽

pp. 1009-1015 ◽

Cited By ~ 2

Author(s):

J. P. Bali ◽

H. Mattras ◽

A. Previero ◽

M. A. Coletti-Previero

Keyword(s):

Biological Activity ◽

Amino Acid ◽

Aromatic Amino Acid ◽

Aminopeptidase Activity ◽

Proteolytic Degradation ◽

Short Peptides ◽

Rat Blood ◽

Active Peptides

Rat blood was shown to contain an aminopeptidase which rapidly hydrolyses short peptides containing an aromatic amino acid as N-terminal residue. Using tetragastrin (Trp-Met-Asp-PheNH 2) as substrate, we showed that some amino acid hydroxamates inhibit rat aminopeptidase activity ‘in vitro’ in the following order: HTrpNHOH > HPheNHOH ≫ HAIaNHOH. The same hydroxamates markedly enhanced the biological activity of tetragastrin ‘in vivo’. The amplification of the secretory effect, correlated with the amount of the hydroxamate used, strongly suggests that these compounds can stabilize a number of active peptides in vivo by inhibiting their proteolytic degradation.

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Complete Amino Acid Sequence Determination of Rat Epidermal Growth Factor:Characterization of a Truncated Form with Full In Vitro Biological Activity

Proteins ◽

10.1007/978-1-4613-1787-6_4 ◽

1987 ◽

pp. 37-44

Author(s):

Edouard C. Nice ◽

John A. Smith ◽

Robert L. Moritz ◽

Michael J. O’Hare ◽

Philip S. Rudland ◽

...

Keyword(s):

Biological Activity ◽

Amino Acid ◽

Amino Acid Sequence ◽

Sequence Determination ◽

Truncated Form ◽

Complete Amino Acid Sequence ◽

Epidermal Growth

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Synthesis of New 6,7(N,O)-Heterocyclic 1,4-Naphthoquinones

Biointerface Research in Applied Chemistry ◽

10.33263/briac116.1390313910 ◽

2021 ◽

Vol 11 (6) ◽

pp. 13903-13910

Keyword(s):

Amino Acid ◽

High Activity ◽

Biologically Active ◽

Amino Acid Derivatives ◽

Antimicrobial Substances ◽

Derivatives Of

As a result of the carried out research it was synthesized an order of new potentially biologically active modified N-,O-contained heterocycles on the base of amino acid derivatives of 2,6,7-nitrogen substituted-3-chloro-1,4-naphthoquinone. It was established that among synthesized compounds, there are potential antimicrobial substances with high activity.

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