Ru(II)-Based Amino Acid Complexes Show Promise for Leukemia Treatment: Cytotoxicity and Some Light on their Mechanism of Action

2019 ◽  
Vol 197 (1) ◽  
pp. 123-131
Author(s):  
Aliny Pereira de Lima ◽  
Marcio Aurélio Pinheiro Almeida ◽  
Francyelli Mello-Andrade ◽  
Flávia de Castro Pereira ◽  
Wanessa Carvalho Pires ◽  
...  
2007 ◽  
Vol 115 (S 1) ◽  
Author(s):  
K Stadlbauer ◽  
B Brunmair ◽  
Z Szöcs ◽  
M Krebs ◽  
A Luger ◽  
...  

Diabetes ◽  
1980 ◽  
Vol 29 (10) ◽  
pp. 782-787 ◽  
Author(s):  
F. M. Ng ◽  
J. Bornstein ◽  
C. E. Pullin ◽  
J. O. Bromley ◽  
S. L. Macaulay

1985 ◽  
Vol 104 (1) ◽  
pp. 63-67 ◽  
Author(s):  
I.L. Ulanovski ◽  
A.A. Kurganov ◽  
V.A. Davankov

1971 ◽  
Vol 246 (22) ◽  
pp. 6855-6866 ◽  
Author(s):  
Christopher T. Walsh ◽  
Agnes Schonbrunn ◽  
Robert H. Abeles

Biomolecules ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 421
Author(s):  
Areetha R. D’Souza ◽  
Matthew R. Necelis ◽  
Alona Kulesha ◽  
Gregory A. Caputo ◽  
Olga V. Makhlynets

Antimicrobial peptides (AMPs) present a promising scaffold for the development of potent antimicrobial agents. Substitution of tryptophan by non-natural amino acid Azulenyl-Alanine (AzAla) would allow studying the mechanism of action of AMPs by using unique properties of this amino acid, such as ability to be excited separately from tryptophan in a multi-Trp AMPs and environmental insensitivity. In this work, we investigate the effect of Trp→AzAla substitution in antimicrobial peptide buCATHL4B (contains three Trp side chains). We found that antimicrobial and bactericidal activity of the original peptide was preserved, while cytocompatibility with human cells and proteolytic stability was improved. We envision that AzAla will find applications as a tool for studies of the mechanism of action of AMPs. In addition, incorporation of this non-natural amino acid into AMP sequences could enhance their application properties.


Molecules ◽  
2021 ◽  
Vol 26 (14) ◽  
pp. 4331
Author(s):  
David B. Hobart ◽  
Michael A. G. Berg ◽  
Hannah M. Rogers ◽  
Joseph S. Merola

The reaction of palladium(II) acetate with acyclic amino acids in acetone/water yields square planar bis-chelated palladium amino acid complexes that exhibit interesting non-covalent interactions. In all cases, complexes were examined by multiple spectroscopic techniques, especially HRMS (high resolution mass spectrometry), IR (infrared spectroscopy), and 1H NMR (nuclear magnetic resonance) spectroscopy. In some cases, suitable crystals for single crystal X-ray diffraction were able to be grown and the molecular structure was obtained. The molecular geometries of the products are discussed. Except for the alanine complex, all complexes incorporate water molecules into the extended lattice and exhibit N-H···O and/or O···(HOH)···O hydrogen bonding interactions. The non-covalent interactions are discussed in terms of the extended lattice structures exhibited by the structures.


1989 ◽  
Vol 165 (1) ◽  
pp. 131-137 ◽  
Author(s):  
M. Vicens ◽  
J.J. Fiol ◽  
A. Terron ◽  
V. Moreno

Polyhedron ◽  
1990 ◽  
Vol 9 (5) ◽  
pp. 665-668 ◽  
Author(s):  
F. Rey ◽  
J.M. Antelo ◽  
F. Arce ◽  
F.J. Penedo

1987 ◽  
Vol 118 (11) ◽  
pp. 1289-1296 ◽  
Author(s):  
M. R. Mahmoud ◽  
S. A. El-Gyar ◽  
A. Shaker ◽  
A. M. Abdel-Mawgoud

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