Synthesis, characterization, equilibrium studies, and biological activity of complexes involving copper(II), 2-aminomethylthiophenyl-4-bromosalicylaldehyde Schiff base, and selected amino acids

2014 ◽  
Vol 67 (5) ◽  
pp. 870-890 ◽  
Author(s):  
Mutlaq S. Aljahdali ◽  
Abeer T. Abedelkarim ◽  
Ahmed A. El-Sherif ◽  
Mahmoud M. Ahmed
1993 ◽  
Vol 58 (5) ◽  
pp. 1103-1108 ◽  
Author(s):  
Mohamed M. Shoukry ◽  
Eman M. Shoukry

The formation constants of the binary and ternary complexes of palladium(II) with diethylenetriamine and amino acids as ligands have been determined potentiometrically at 25 °C in 0.1 M NaNO3 solution. The relative stability of each ternary complex was compared with that of the corresponding binary complexes in terms of ∆logK values. The mode of chelation was ascertained by conductivity measurements.


1988 ◽  
Vol 53 (11) ◽  
pp. 2914-2919 ◽  
Author(s):  
Pierrette Maes ◽  
Annie Ricouart ◽  
Emmanuel Escher ◽  
André Tartar ◽  
Christian Sergheraert

Analogs of angiotensin II in which phenylalanine in position 8 was replaced with cymantrenylalanine or with its triphenylphosphine photosubstitution product were synthesized by the solid-phase method. On rabbit aorta strips, these peptides were found to be pure antagonists of angiotensin II. Their relative affinities are higher than most other analogs substituted in position 8 with bulky amino-acids.


2021 ◽  
Vol 330 ◽  
pp. 115522
Author(s):  
Ola A. El-Gammal ◽  
Farid Sh. Mohamed ◽  
Ghada N. Rezk ◽  
Ashraf A. El-Bindary

2019 ◽  
Vol 48 (18) ◽  
pp. 5987-6002 ◽  
Author(s):  
A. Paden King ◽  
Hendryck A. Gellineau ◽  
Samantha N. MacMillan ◽  
Justin J. Wilson

A subset of fluorinated Co(iii) Schiff base complexes was synthesized, and their structural, ligand exchange, and anticancer properties were investigated.


1988 ◽  
Vol 8 (3) ◽  
pp. 1247-1252 ◽  
Author(s):  
E Lazar ◽  
S Watanabe ◽  
S Dalton ◽  
M B Sporn

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.


2001 ◽  
Vol 21 (1) ◽  
pp. 354-366 ◽  
Author(s):  
Carolina Sousa ◽  
Christina Johansson ◽  
Celine Charon ◽  
Hamid Manyani ◽  
Christof Sautter ◽  
...  

ABSTRACT A diversity of mRNAs containing only short open reading frames (sORF-RNAs; encoding less than 30 amino acids) have been shown to be induced in growth and differentiation processes. The early nodulin geneenod40, coding for a 0.7-kb sORF-RNA, is expressed in the nodule primordium developing in the root cortex of leguminous plants after infection by symbiotic bacteria. Ballistic microtargeting of this gene into Medicago roots induced division of cortical cells. Translation of two sORFs (I and II, 13 and 27 amino acids, respectively) present in the conserved 5′ and 3′ regions ofenod40 was required for this biological activity. These sORFs may be translated in roots via a reinitiation mechanism. In vitro translation products starting from the ATG of sORF I were detectable by mutating enod40 to yield peptides larger than 38 amino acids. Deletion of a Medicago truncatula enod40 region between the sORFs, spanning a predicted RNA structure, did not affect their translation but resulted in significantly decreased biological activity. Our data reveal a complex regulation of enod40action, pointing to a role of sORF-encoded peptides and structured RNA signals in developmental processes involving sORF-RNAs.


2002 ◽  
Vol 38 (5) ◽  
pp. 989-999 ◽  
Author(s):  
Rosica Mladenova ◽  
Milena Ignatova ◽  
Nevena Manolova ◽  
Tsvetanka Petrova ◽  
Iliya Rashkov

1998 ◽  
Vol 33 (4) ◽  
pp. 331-334 ◽  
Author(s):  
Irina Bobrova ◽  
Natalia Mishlakova ◽  
Anette Selander ◽  
Elena Mekshun ◽  
Guntis Rozental

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