[5-Aspartic acid]-oxytocin: first 5-position neurohypophyseal hormone analog possessing significant biological activity

1978 ◽  
Vol 100 (3) ◽  
pp. 972-973 ◽  
Author(s):  
Roderich Walter ◽  
Gerald Skala ◽  
Clark W. Smith
Keyword(s):  
Biological Activity ◽  
Aspartic Acid ◽  
Hormone Analog ◽  
Neurohypophyseal Hormone

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

1988 ◽  
Vol 8 (3) ◽  
pp. 1247-1252 ◽  
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.

In Vivo Biological Activity of a Recombinant Salmon Follicle-Stimulating Hormone Analog in Prepubertal Male Coho Salmon.

2010 ◽  
Vol 83 (Suppl_1) ◽  
pp. 574-574
Author(s):  
Koichiro Gen ◽  
Jon T. Dickey ◽  
J. Adam Luckenbach ◽  
Yoji Yamamoto ◽  
Olga Mirochnitchenko ◽  
...  
Keyword(s):  
Biological Activity ◽  
Coho Salmon ◽  
Follicle Stimulating Hormone ◽  
Hormone Analog ◽  
Stimulating Hormone

scholarly journals Solid-State Synthesis, Characterization, and Biological Activity of the Bioinorganic Complex of Aspartic Acid and Arsenic Triiodide

2013 ◽  
Vol 2013 ◽  
pp. 1-5 ◽  
Author(s):  
Guo-Qing Zhong ◽  
Wen-Wei Zhong ◽  
Rong-Rong Jia ◽  
Yu-Qing Jia
Keyword(s):  
Crystal Structure ◽  
Biological Activity ◽  
Solid State ◽  
Complex Formation ◽  
Aspartic Acid ◽  
Infrared Spectra ◽  
Room Temperature ◽  
Biological Test ◽  
Bridge Structure ◽  
Monoclinic System

The bioinorganic complex of aspartic acid and arsenic triiodide was synthesized by a solid-state reaction at room temperature. The formula of the complex is AsI3[HOOCCH2CH(NH2)COOH]2.5. The crystal structure of the complex belongs to monoclinic system with lattice parameters:a=1.0019 nm,b=1.5118 nm,c=2.1971 nm, andβ=100.28°. The infrared spectra can demonstrate the complex formation between the arsenic ion and aspartic acid, and the complex may be a dimer with bridge structure. The result of primary biological test indicates that the complex possesses better biological activity for the HL-60 cells of the leukemia than arsenic triiodide.

Synthesis, physicochemical characterization and biological activity of nano complexes of iron(III) of 3(2'-hydroxyphenyl)-5-(4′-substituted phenyl) pyrazolines and aspartic acid

2012 ◽  
Vol 26 (5) ◽  
pp. 203-211 ◽  
Author(s):  
Afshan Siddiqui ◽  
Kajal Singh ◽  
Kanchan Lata Singh ◽  
Shailendra Kumar Gupta ◽  
Mohd Safi Ahmad ◽  
...  
Keyword(s):  
Biological Activity ◽  
Aspartic Acid ◽  
Physicochemical Characterization

scholarly journals A correlation study of biological activity and molecular docking of Asp and Glu linked bis-hydrazones of quinazolinones

RSC Advances ◽  
2018 ◽  
Vol 8 (19) ◽  
pp. 10644-10653 ◽  
Author(s):  
H. K. Kumara ◽  
R. Suhas ◽  
D. M. Suyoga Vardhan ◽  
M. Shobha ◽  
D. Channe Gowda
Keyword(s):  
Biological Activity ◽  
Molecular Docking ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Correlation Study

The present investigation involves the synthesis and spectroscopic and biological activity studies of the bis-hydrazones of quinazolinones derived from aspartic acid and glutamic acid.

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

1988 ◽  
Vol 8 (3) ◽  
pp. 1247-1252
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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