Synthesis and Biological Activity of Four Vasopressin Analogs Modified in Position 3 with β-Thienylalanine

1995 ◽  
Vol 60 (4) ◽  
pp. 681-686 ◽  
Author(s):  
Jiřina Slaninová ◽  
Malgorzata Czaja ◽  
Bernard Lammek
Keyword(s):  
Biological Activity ◽  
Arginine Vasopressin ◽  
Peptide Bonds

Four new analogs of arginine-vasopressin substituted in position 3 with β-thienylalanine were synthesized on chloromethylated resin using Boc strategy and DCC or DCC-HOBt to form peptide bonds. The activity of the agonists is not much different in comparison to the unsubstituted compounds. However, the potency of one of the antagonists is strongly reduced.

THE DEVELOPMENT OF A RADIOIMMUNOASSAY FOR OXYTOCIN: SENSITIVITY OF THE ASSAY IN AQUEOUS BUFFER SOLUTION, SPECIFICITY AND THE DISSOCIATION OF IMMUNOLOGICAL AND BIOLOGICAL ACTIVITY

1970 ◽  
Vol 46 (4) ◽  
pp. 533-542 ◽  
Author(s):  
T. CHARD ◽  
M. L. FORSLING ◽  
M. A. R. JAMES ◽  
M. J. KITAU ◽  
J. LANDON
Keyword(s):  
Aqueous Solution ◽  
Biological Activity ◽  
Arginine Vasopressin ◽  
Late Pregnancy ◽  
Reducing Agents ◽  
Immunological Activity ◽  
Buffer Solution ◽  
Aqueous Buffer ◽  
Lysine Vasopressin ◽  
Other Substances

SUMMARY A radioimmunoassay for oxytocin in aqueous solution is described, with a sensitivity comparable with the best current bioassays. It is highly specific; arginine-vasopressin and lysine-vasopressin interfere only at 1000-fold greater concentration, while bradykinin, histamine, acetycholine and many other substances, which interfere with some bioassays, have no effect. In certain circumstances, there is a dissociation between loss of biological and immunological activity. Thus reducing agents had no effect on immunological activity, in contrast to their effect on biological activity. In late pregnancy plasma, the biological activity of oxytocin is destroyed more rapidly than the immunological activity. Radioimmunoassays have considerable advantages over bioassays both in convenience and specificity. However, bioassays should be employed for reference purposes because of the dissociation between biological and immunological activity that may occur.

Effect of N-methylation of selected peptide bonds on the biological activity of insulin. [2-N-Methylisoleucine-A]insulin

2009 ◽  
Vol 30 (4) ◽  
pp. 460-473 ◽  
Author(s):  
HIROSHI OGAWA ◽  
G. THOMPSON BURKE ◽  
JACOB D. CHANLEY ◽  
PANAYOTIS G. KATSOYANNIS
Keyword(s):  
Biological Activity ◽  
Peptide Bonds

Synthesis, biological activity and receptor binding affinity of two [8-arginine]vasopressin analogues with inhibitory properties

1988 ◽  
Vol 53 (11) ◽  
pp. 2907-2913 ◽  
Author(s):  
Franciszek Kasprzykowski ◽  
Zbigniew Grzonka ◽  
Jiřina Slaninová ◽  
Tomislav Barth ◽  
Peter Crause ◽  
...  
Keyword(s):  
Biological Activity ◽  
Arginine Vasopressin ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Synthesis Method ◽  
The Other ◽  
Binding Affinities ◽  
Bovine Kidney ◽  
Liver Membranes ◽  
Vasopressin Analogues

Two analogues of arginine-vasopressin: [1-(β-mercapto-β,β-cyclopentamethylenepropionic acid), 2-D-phenylalanine, 7-sarcosine, 8-arginine]vasopressin and [1-(β-mercapto-β,β-cyclopentamethylenepropionic acid), 2-D-phenylalanine, 7-N-methylalanine, 8-arginine]vasopressin were synthesized by solid-phase peptide synthesis method. Both peptides exhibit antioxytocic, antivasopressor and antiglycogenolytic activities, and on the other hand they are weak antidiuretic agonists. The binding affinities of both analogues to oxytocic receptor (guinea pig myometrium membranes) and to hepatic V1 receptor (rat liver membranes) are practically the same as for the parent hormones, whereas the binding affinities to renal V2 receptor (bovine kidney membranes) are 60-90 times lower than for vasopressin.

The preparation and metabolic fate of tritiated Nα-acetyl[2-O-methyltyrosine]oxytocin - An inhibitor of the uterotonic action of oxytocin

1979 ◽  
Vol 44 (9) ◽  
pp. 2702-2709
Author(s):  
Vera Bojanovska ◽  
Tomislav Barth ◽  
Bohuslav Černý ◽  
Karel Hauzer ◽  
Karel Jošt
Keyword(s):  
Biological Activity ◽  
Mammary Gland ◽  
Specific Radioactivity ◽  
Subcellular Fractions ◽  
Metabolic Fate ◽  
Rat Uterus ◽  
Peptide Bonds ◽  
Human Pregnancy ◽  
Metabolic Products

An inhibitor of the uterotonic action of oxytocin-[CH3CO-3H] [2-O-methyltyrosine]oxytocin - having biological activity and a specific radioactivity of 3-7 Ci/mmol was prepared by the reaction of [2-O-methyltyrosine]oxytocin with 2,2'-3H2-acetanhydride. The analogue was stable in human pregnancy serum. Chymotrypsin split the Tyr(Me)-Ile and Leu-GlyNH2 peptide bonds. In the presence of subcellular fractions of homogenates of the rat uterus and mammary gland, several metabolic products were formed from the analogue.

Synthesis and properties of analogues of vasopressin with 1-aminocyclopropane-1-carboxylic acid in position 9

1988 ◽  
Vol 53 (11) ◽  
pp. 2604-2616 ◽  
Author(s):  
Zdenko Procházka ◽  
Juris E. Ancans ◽  
Jiřina Slaninová ◽  
Alena Machová ◽  
Tomislav Barth ◽  
...  
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Nmr Spectroscopy ◽  
Carboxylic Acid ◽  
Arginine Vasopressin ◽  
Solid Phase ◽  
Biological Activities ◽  
Solution Conformation ◽  
Lysine Vasopressin ◽  
C Nmr

Solid phase methodology on benzhydrylamine resin was used for the synthesis of three analogues of vasopressin with non-coded amino acid, 1-aminocyclopropane 1-carboxylic acid, in position 9. Two analogues of lysine-vasopressin ([Lys8, Acc9]vasopressin (I) and Gly3-[Lys8, Acc9]vasopressin (II)) and one analogue of arginine-vasopressin ([Arg8, Acc9]vasopressin (III)) have been synthesized. The dubious value of the biological activity of [Lys8, D-Ala9]vasopressin was reevaluated and [Lys8, L-Ala9]vasopressin was also synthesized and tested for the comparison. Differences in solution conformation of these two analogues were studied by 1H and 13C NMR spectroscopy. Biological activities of all analogues were either significantly lowered or almost completely eliminated. Analogues I-III were found to be completely inactive in analgesia and the CNS activities tested (active and passive avoidance).

scholarly journals BIOLOGICAL ACTIVITY OF THE CLEAVAGE PRODUCT OF HUMAN IMMUNOGLOBULIN G WITH CYANOGEN BROMIDE

1967 ◽  
Vol 125 (5) ◽  
pp. 787-805 ◽  
Author(s):  
Mira Lahav ◽  
Ruth Arnon ◽  
Michael Sela
Keyword(s):  
Biological Activity ◽  
Cyanogen Bromide ◽  
Biological Activities ◽  
Gel Filtration ◽  
Cleavage Product ◽  
The Other ◽  
Antibody Activity ◽  
Peptide Bonds ◽  
Binding Reaction ◽  
Therapeutic Uses

Treatment of human IgG with cyanogen bromide in 0.05 M HCl under specified conditions resulted in the cleavage of about half of its methionyl peptide bonds. A major fragment of about 5S was isolated from the reaction mixture by gel filtration in quantitative yield. The CNBr fragment reacted fully with goat antiserum against human light chain, but its reaction with anti-heavy chain was markedly decreased. The treatment with CNBr caused a drastic decrease in the following biological activities of IgG: complement fixing, skin binding, reaction with antiglobulin factors, and reaction with specific anti-Gm(12) serum. On the other hand, the reaction with serum of anti-Gm(1) or anti-Gm(4) specificity was not impaired and antibody activity, namely antistreptolysin and isohemagglutinin, was retained after the treatment with CNBr. It is concluded that the CNBr cleaves preferentially the methionyl bonds in the Fc portion of IgG, and that the major fragment obtained, denoted F(ab'')2, has still the combining properties of a divalent antibody. The possible therapeutic uses of F(ab'')2 are discussed.

Loss of biological activity of arginine vasopressin during its degradation by vasopressinase from pregnancy serum

1995 ◽  
Vol 42 (1) ◽  
pp. 51-58 ◽  
Author(s):  
M. P. Gordge ◽  
D. J. Williams ◽  
N. J. Huggett ◽  
N. N. Payne ◽  
G. H. Nelld
Keyword(s):  
Biological Activity ◽  
Arginine Vasopressin
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