scholarly journals Back Cover: Corrole and Porphyrin Amino Acid Conjugates: Synthesis and Physicochemical Properties (Chem. Eur. J. 32/2016)

2016 ◽  
Vol 22 (32) ◽  
pp. 11472-11472
Author(s):  
Kostas Karikis ◽  
Evangelos Georgilis ◽  
Georgios Charalambidis ◽  
Athanasia Petrou ◽  
Olena Vakuliuk ◽  
...  
2016 ◽  
Vol 22 (32) ◽  
pp. 11245-11252 ◽  
Author(s):  
Kostas Karikis ◽  
Evangelos Georgilis ◽  
Georgios Charalambidis ◽  
Athanasia Petrou ◽  
Olena Vakuliuk ◽  
...  

2020 ◽  
Vol 17 (1) ◽  
pp. 71-84
Author(s):  
Riham M. Bokhtia ◽  
Siva S. Panda ◽  
Adel S. Girgis ◽  
Hitesh H. Honkanadavar ◽  
Tarek S. Ibrahim ◽  
...  

Background: Bacterial infections are considered as one of the major global health threats, so it is very essential to design and develop new antibacterial agents to overcome the drawbacks of existing antibacterial agents. Method: The aim of this work is to synthesize a series of new fluoroquinolone-3-carboxamide amino acid conjugates by molecular hybridization. We utilized benzotriazole chemistry to synthesize the desired hybrid conjugates. Result: All the conjugates were synthesized in good yields, characterized, evaluated for their antibacterial activity. The compounds were screened for their antibacterial activity using methods adapted from the Clinical and Laboratory Standards Institute. Synthesized conjugates were tested for activity against medically relevant pathogens; Escherichia coli (ATCC 25922), Pseudomonas aeruginosa (ATCC 27856) Staphylococcus aureus (ATCC 25923) and Enterococcus faecalis (ATCC 19433). Conclusion: The observed antibacterial experimental data indicates the selectivity of our synthesized conjugates against E.Coli. The protecting group on amino acids decreases the antibacterial activity. The synthesized conjugates are non-toxic to the normal cell lines. The experimental data were supported by computational studies.


2020 ◽  
Vol 14 (3) ◽  
pp. 235-246
Author(s):  
Sara Abdollahi ◽  
Mohammad H. Morowvat ◽  
Amir Savardashtaki ◽  
Cambyz Irajie ◽  
Sohrab Najafipour ◽  
...  

Background: Arginine deiminase is a bacterial enzyme, which degrades L-arginine. Some human cancers such as hepatocellular carcinoma (HCC) and melanoma are auxotrophic for arginine. Therefore, PEGylated arginine deiminase (ADI-PEG20) is a good anticancer candidate with antitumor effects. It causes local depletion of L-arginine and growth inhibition in arginineauxotrophic tumor cells. The FDA and EMA have granted orphan status to this drug. Some recently published patents have dealt with this enzyme or its PEGylated form. Objective: Due to increasing attention to it, we aimed to evaluate and compare 30 arginine deiminase proteins from different bacterial species through in silico analysis. Methods: The exploited analyses included the investigation of physicochemical properties, multiple sequence alignment (MSA), motif, superfamily, phylogenetic and 3D comparative analyses of arginine deiminase proteins thorough various bioinformatics tools. Results: The most abundant amino acid in the arginine deiminase proteins is leucine (10.13%) while the least amino acid ratio is cysteine (0.98%). Multiple sequence alignment showed 47 conserved patterns between 30 arginine deiminase amino acid sequences. The results of sequence homology among 30 different groups of arginine deiminase enzymes revealed that all the studied sequences located in amidinotransferase superfamily. Based on the phylogenetic analysis, two major clusters were identified. Considering the results of various in silico studies; we selected the five best candidates for further investigations. The 3D structures of the best five arginine deiminase proteins were generated by the I-TASSER server and PyMOL. The RAMPAGE analysis revealed that 81.4%-91.4%, of the selected sequences, were located in the favored region of arginine deiminase proteins. Conclusion: The results of this study shed light on the basic physicochemical properties of thirty major arginine deiminase sequences. The obtained data could be employed for further in vivo and clinical studies and also for developing the related therapeutic enzymes.


2020 ◽  
Vol 18 (15) ◽  
pp. 2877-2885
Author(s):  
Faisal Hayat ◽  
Marie E. Migaud

O5′ amino acid ester conjugates of nicotinamide riboside, generated via a reduced intermediate, are stable to purine nucleoside phosphorylase.


2014 ◽  
Vol 2014 (8) ◽  
pp. 1741-1752 ◽  
Author(s):  
Karen Wright ◽  
Edouard d'Aboville ◽  
Joseph Scola ◽  
Tommaso Margola ◽  
Antonio Toffoletti ◽  
...  

Amino Acids ◽  
1999 ◽  
Vol 16 (3-4) ◽  
pp. 425-440 ◽  
Author(s):  
M. H. Abo-Ghalia ◽  
A. M. Shalaby ◽  
W. I. El-Eraqi ◽  
H. M. Awad

2013 ◽  
Vol 3 (3) ◽  
pp. 241-246 ◽  
Author(s):  
S.K. Sharma ◽  
C. Karthikeyan ◽  
N.S. Hari Narayana Moorthy ◽  
D.K. Jain ◽  
P. Trivedi

2001 ◽  
pp. 493-534 ◽  
Author(s):  
Jacquelyn Gervay-Hague ◽  
Thomas Weathers Jr

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