Mixed-ligand copper(ii) Schiff base complexes: the vital role of co-ligands in DNA/protein interactions and cytotoxicity

2017 ◽  
Vol 41 (3) ◽  
pp. 1267-1283 ◽  
Author(s):  
Sellamuthu Kathiresan ◽  
Subramanian Mugesh ◽  
Jamespandi Annaraj ◽  
Maruthamuthu Murugan
Keyword(s):  
Cell Death ◽  
Cell Wall ◽  
Schiff Base ◽  
Protein Interactions ◽  
Apoptotic Cell ◽  
Vital Role ◽  
Mixed Ligand ◽  
Schiff Base Complexes ◽  
Antibacterial Mechanism

Four new mixed-ligand copper(ii) complexes display an antibacterial mechanism of cell death via cell-wall rupture and cytotoxicity via apoptotic cell death.

Mixed-ligand copper(ii) Schiff base complexes: the role of the co-ligand in DNA binding, DNA cleavage, protein binding and cytotoxicity

2016 ◽  
Vol 45 (22) ◽  
pp. 9073-9087 ◽  
Author(s):  
Wen-Jing Lian ◽  
Xin-Tian Wang ◽  
Cheng-Zhi Xie ◽  
He Tian ◽  
Xue-Qing Song ◽  
...  
Keyword(s):  
Schiff Base ◽  
Dna Binding ◽  
Protein Binding ◽  
Dna Cleavage ◽  
Mixed Ligand ◽  
Schiff Base Complexes ◽  
Biological Features

Four novel mixed-ligand copper(ii) Schiff base complexes were synthesized and characterized. The biological features of the complexes and how acetic auxiliary ligands manipulate these features were investigated.

Homology Modeling and Docking Studies of Bcl-2 and Bcl-xL with Small Molecule Inhibitors: Identification and Functional Studies

2019 ◽  
Vol 18 (31) ◽  
pp. 2633-2663 ◽  
Author(s):  
Abdul Ajees Abdul Salam ◽  
Upendra Nayek ◽  
Dhanya Sunil
Keyword(s):  
Cell Death ◽  
Homology Modeling ◽  
Apoptotic Cell ◽  
Docking Studies ◽  
Vital Role ◽  
Potential Drug ◽  
X Ray Crystallography ◽  
Functional Studies ◽  
Drug Molecules

Apoptosis is a vital physiological process, which is observed in various biological events. The anti-apoptotic and pro-apoptotic members of Bcl-2 family are the most characterized proteins which are involved in the regulation of apoptotic cell death. The anti-apoptotic proteins such as Bcl-2 and Bcl-xL prevent apoptosis, whereas pro-apoptotic members like Bax and Bak, elicit the release of caspases from death antagonists inducing apoptosis. Thus, the Bcl-2 family of proteins play a vital role in controlling programmed cell death. Over expression of anti-apoptotic Bcl-2 proteins are often directly associated with various kinds of cancer. Developing suitable inhibitors for controlling the elevated levels of these proteins got much attention in last decade. Structural biology techniques such as Nuclear Magnetic Resonance (NMR) spectroscopy, X-ray crystallography, homology modeling and molecular docking play a significant role in identifying the key inhibitors of these proteins. The authors have developed and tested successfully, several series of indole pharmacore containing inhibitors for Bcl-2 and Bcl-xL proteins based on the homology modeling, docking and suitable biochemical and apoptosis assays. This review provides a summary of potential inhibitor molecules developed for Bcl-2 and Bcl-xL proteins, as well as the the key residues of these proteins interacting with potential drug molecules. The present appraisal also focuses on the role of computational algorithms in developing potential drug molecules,with more emphasis on the role of homology modeling and docking studies in developing inhibitors for Bcl- 2, and Bcl-xL proteins in cancer therapy.

Syntheses, characterizations, crystal structures, and biological activities of two new mixed ligand Ni(II) and Cu(II) Schiff base complexes

2015 ◽  
Vol 68 (4) ◽  
pp. 632-649 ◽  
Author(s):  
S. Yousef Ebrahimipour ◽  
Maryam Mohamadi ◽  
Jesús Castro ◽  
Nasrin Mollania ◽  
Hadi Amiri Rudbari ◽  
...  
Keyword(s):  
Schiff Base ◽  
Crystal Structures ◽  
Biological Activities ◽  
Mixed Ligand ◽  
Schiff Base Complexes

scholarly journals Mitochondria: Regulators of Cell Death and Survival

2002 ◽  
Vol 2 ◽  
pp. 1569-1578 ◽  
Author(s):  
David J. Granville ◽  
Roberta A. Gottlieb
Keyword(s):  
Cell Death ◽  
Conformational Changes ◽  
Protein Interactions ◽  
Apoptotic Cell ◽  
Critical Role ◽  
Death Process ◽  
Protein Protein Interactions ◽  
Ionic Changes ◽  
A Cell ◽  
Cyt C

The past 5 years has seen an intense surge in research devoted toward understanding the critical role of mitochondria in the regulation of cell death. Apoptosis can be initiated by a wide array of stimuli, inducing multiple signaling pathways that, for the most part, converge at the mitochondrion. Although classically considered the powerhouses of the cell, it is now understood that mitochondria are also “gatekeepers” that ultimately determine the fate of the cell. The mitochondrial decision as to whether a cell lives or dies is complex, involving protein-protein interactions, ionic changes, reactive oxygen species, and other mechanisms that require further elucidation. Once the death process is initiated, mitochondria undergo conformational changes, resulting in the release of cytochrome c (cyt c), caspases, endonucleases, and other factors leading to the onset and execution of apoptosis. The present review attempts to outline the complex milieu of events regulating the mitochondrial commitment to and processes involved in the implementation of the executioner phase of apoptotic cell death.

scholarly journals Cell wall dynamics modulate acetic acid-induced apoptotic cell death of Saccharomyces cerevisiae

2014 ◽  
Vol 1 (9) ◽  
pp. 303-314 ◽  
Author(s):  
Antonio Rego ◽  
◽  
Ana Duarte ◽  
Flavio Azevedo ◽  
Maria Sousa ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Death ◽  
Cell Wall ◽  
Acetic Acid ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death

scholarly journals Caspase-9 cleavage, do you need it?

2007 ◽  
Vol 405 (1) ◽  
Author(s):  
Davina Twiddy ◽  
Kelvin Cain
Keyword(s):  
Cell Death ◽  
Apoptotic Cell ◽  
Caspase 9 ◽  
Autocatalytic Cleavage ◽  
Downstream Effector ◽  
Apoptosis Inhibition ◽  
Biochemical Journal ◽  
Effector Caspase ◽  
Effector Caspases

Caspase-9, which is activated by association with the Apaf-1 (apoptotic protease-activating factor-1) apoptosome complex, cleaves and activates the downstream effector caspases-3 and -7, thereby executing the caspase-cascade and cell-death programme. Although caspase-9 does not need to be cleaved to be active, apoptotic cell death is always accompanied by autocatalytic cleavage and by further downstream effector caspase-dependent cleavage of caspase-9. In this issue of the Biochemical Journal, Denault and co-workers evaluate the role of caspase-3-dependent cleavage of caspase-9 and conclude that this mechanism mainly serves to enhance apoptosis by alleviating XIAP (X-linked inhibitor of apoptosis) inhibition of the apical caspase.

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