Antagonists of angiotensin II containing N-methyl-L-alanine and DL-nipecotic acid in position 7

1979 ◽  
Vol 57 (7) ◽  
pp. 763-766 ◽  
Author(s):  
Graham J. Moore ◽  
Evelyn M. Ko
Keyword(s):  
Angiotensin Ii ◽  
Solid Phase ◽  
Exchange Chromatography ◽  
Phase Method ◽  
Rat Uterus ◽  
Nipecotic Acid ◽  
Solid Phase Method ◽  
Pressor Activity ◽  
Secondary Amino ◽  
Myotropic Activity

[1-sarcosine, 7-N-methyl-L-alanine, 8-isoleucine]-Angiotensin II and [1-sarcosine, 7-DL-nipecotic acid, 8-isoleucine]-angiotensin II were synthesized by the solid-phase method and purified by cation-exchange chromatography and high-pressure liquid chromatography. In the isolated rat uterus these analogs and < 0.1% of the myotropic activity of angiotensin II and inhibited angiotensin II with pA2 values of 8.2 and 7.8, respectively. In the rat pressor assay (vagotomized ganglion blocked rat) these analogs had 0.9 and 2.8%, respectively, of the pressor activity of angiotensin II. The results show that the proline residue in position 7 of [Sar1,Ile8]-angiotensin II may be replaced by other secondary amino acids without disrupting interactions at angiotensin II receptors.

Synthesis and biological activity of new metallocenic angiotensin II analogs

1988 ◽  
Vol 53 (11) ◽  
pp. 2914-2919 ◽  
Author(s):  
Pierrette Maes ◽  
Annie Ricouart ◽  
Emmanuel Escher ◽  
André Tartar ◽  
Christian Sergheraert
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Angiotensin Ii ◽  
Solid Phase ◽  
Rabbit Aorta ◽  
Phase Method ◽  
Solid Phase Method

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.

Synthesis and solution conformation of [Trp1, Val5]-angiotensin II

1977 ◽  
Vol 55 (1) ◽  
pp. 75-82 ◽  
Author(s):  
Peter W. Schiller
Keyword(s):  
Angiotensin Ii ◽  
Solid Phase ◽  
Fluorescence Emission ◽  
Resonance Energy ◽  
Tryptophan Fluorescence ◽  
Exchange Chromatography ◽  
Phase Method ◽  
Aqueous Environment ◽  
Solution Conformation ◽  
Intramolecular Distance

[Trp1, Val5]-Angiotensin II was synthesized by the solid-phase method and purified by partition chromatography on Sephadex G-25 and by ion-exchange chromatography on Sephadex SP-25. Relative to [Val5]-angiotensin II, the analog displayed 36% smooth muscle activity in a preparation of the superior mesenteric artery. Conformational aspects of the analog were revealed by fluorescence techniques. The fluorescence emission maximum at 350 nm suggests a completely aqueous environment for the tryptophanyl residue in [Trp1, Val5]-angiotensin II. Singlet–singlet resonance energy transfer between Tyr in position 4 and Trp in position 1 was evaluated for a calculation of the intramolecular distance between these two residues on the basis of the Förster equation. From the relative increase of tryptophan fluorescence a transfer efficiency of > 0.9 was obtained, which is compatible with the observed complete quenching of tyrosine fluorescence in the analog. The computed average intramolecular distance of < 8 Å precludes an extended conformation for the N-terminal sequence encompassing residues 1 through 4 at neutral pH and suggests the existence of a loop in this part of the molecule. The results are discussed in relation to the various models proposed for the solution conformation of angiotensin II.

Antagonistic Analogs of Oxytocin with Substituted Phenylalanine or Tyrosine in Position 2

1994 ◽  
Vol 59 (6) ◽  
pp. 1430-1438 ◽  
Author(s):  
Rudolf Ježek ◽  
Miroslava Žertová ◽  
Jiřina Slaninová ◽  
Pavel Majer ◽  
Zdenko Procházka
Keyword(s):  
Amino Acids ◽  
Solid Phase ◽  
Phase Method ◽  
Inhibiting Activity ◽  
Structure Activity ◽  
Low Degree ◽  
Solid Phase Method ◽  
Pressor Activity ◽  
Agonistic Activity

Solid phase method on p-methylbenzhydrylamine resin was used for the synthesis of seven analogs of oxytocin with non-coded amino acids in position 2. [L-Phe(4-Me)2]oxytocin (I), [D-Phe(4-Me)2]oxytocin (II), [L-Phe(2-Me,4-Et)2]oxytocin (III), [D-Phe(2-Me,4-Et)2]oxytocin (IV), [D-Tyr(Me)2]oxytocin (V), [D-Tyr(Et)2]oxytocin (VI) and [L-Tyr(2-Me)2]oxytocin (VII) were synthesized. All analogs with D-stereoisomer of alkyl or alkoxy substituted phenylalanine possess uterus in vitro inhibiting activity. In the case of L-stereoisomers the structure activity relationship is more complicated. As far as the pressor activity is concerned, the analogs have either very low agonistic activity or low degree of antagonism.

Synthesis of Peptides with the Solid Phase Method. II. Octapeptide Analogues of Angiotensin II

1974 ◽  
Vol 52 (2) ◽  
pp. 113-119 ◽  
Author(s):  
W. K. Park ◽  
C. Choi ◽  
F. Rioux ◽  
D. Regoli
Keyword(s):  
Blood Pressure ◽  
Biological Activity ◽  
Angiotensin Ii ◽  
Enzymatic Degradation ◽  
Solid Phase ◽  
Paper Electrophoresis ◽  
Antagonistic Effect ◽  
Phase Method ◽  
Solid Phase Method ◽  
Layer Chromatography

Forty-six analogues of angiotensin II were obtained with the solid-phase method for peptide synthesis. The peptides were purified, using the conventional procedures; homogeneity and purity were established after paper, thin-layer chromatography, paper electrophoresis, amino acid analysis, elemental analysis, and enzymatic degradation by aminopeptidase. The biological activity of all compounds was compared with that of angiotensin II on the blood pressure of anesthetized rats. The same test was used to establish the antagonistic effect of several analogues against angiotensin II.

Synthesis of peptides by the solid-phase method. V. Substance P and analogs

1980 ◽  
Vol 58 (4) ◽  
pp. 272-280 ◽  
Author(s):  
A. Fournier ◽  
R. Couture ◽  
J. Magnan ◽  
M. Gendreau ◽  
D. Regoli ◽  
...  
Keyword(s):  
Substance P ◽  
Solid Phase ◽  
Gel Filtration ◽  
Paper Electrophoresis ◽  
Exchange Chromatography ◽  
Phase Method ◽  
Elemental Analyses ◽  
Solid Phase Method

We have synthesized a series of 12 analogs of the undecapeptide substance P in order to perform a structure–activity study of this peptide. In the present work, each residue was substituted by L-alanine, and the C-terminal amide was replaced by the free carboxyl in order to pinpoint biologically important side chains and functional groups. The synthesis of the analogs was carried out by the automatic solid-phase method. Couplings were performed by the symmetrical anhydride procedure. After cleavage with liquid HF, the peptides were purified by gel filtration and ion-exchange chromatography. Their purity was assessed by thin-layer chromatography, paper electrophoresis, amino acid and elemental analyses, and high pressure liquid chromatography. They were tested for biological activity in vitro on the ileum of the guinea pig, the mesenteric vein of the rabbit, and the vas deferens of the rat, and in vivo by measuring their effect on the blood pressure of the rat.

Synthesis of Peptides by the Solid Phase Method. I. Tetradecapeptide Renin Substrate and Intermediate Peptides, Nonapeptides, and Fragments of Angiotensin II

1974 ◽  
Vol 52 (2) ◽  
pp. 106-112 ◽  
Author(s):  
W. K. Park ◽  
C. Choi ◽  
F. Rioux ◽  
D. Regoli
Keyword(s):  
Amino Acid ◽  
Angiotensin Ii ◽  
Enzymatic Degradation ◽  
Solid Phase ◽  
Reaction Vessel ◽  
Phase Method ◽  
Renin Substrate ◽  
Aminopeptidase M ◽  
Solid Phase Method ◽  
Solvent Systems

Tetradecapeptide renin substrate (H∙Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser∙OH) (1–14), tridecapeptide (1–13), dodecapeptide (1–12), undecapeptide (1–11), two nonapeptides (1–9) and (1–9-Leu), heptapeptide (1–7), tetrapeptide (1–4), tetrapeptide (5–8), pentapeptide (4–8), hexapeptide (3–8), and heptapeptide (2–8) were synthesized by the solid phase method and by using an improved reaction vessel. The yield averaged 50–70%. Homogeneity and purity of peptides were established with elemental anlysis for C, H, and N, paper chromatography in three solvent systems, electrophoresis, amino acid analysis, and enzymatic degradation by aminopeptidase M.

Synthesis of modified human C-peptide and its fragments

1988 ◽  
Vol 53 (11) ◽  
pp. 2637-2644 ◽  
Author(s):  
Běla Bendlová ◽  
Michal Lebl ◽  
Pavel Štolba ◽  
Luboslav Stárka
Keyword(s):  
Solid Phase ◽  
Gel Filtration ◽  
Reversed Phase ◽  
Exchange Chromatography ◽  
Phase Method ◽  
Reversed Phase Hplc ◽  
Radioactive Label ◽  
C Peptide ◽  
Solid Phase Method ◽  
Internal Marker

Syntheses of the modified human C-peptide containing residues suitable for the introduction of the radioactive label (tyrosine) and internal marker for monitoring binding to carrier (norvaline) and five of its fragments are described. The syntheses were performed by solid phase method using either 9-fluorenylmethoxycarbonyl or tert-butyloxycarbonyl protecting groups. The products were purified by gel filtration, ion exchange chromatography and reversed phase HPLC. The reactivity of prepared peptides with antisera was determined and the modified C-peptide was found fully reactive.

Synthesis of peptides by the solid-phase method. IV. Des-Arg9-bradykinin and analogs

1979 ◽  
Vol 57 (8) ◽  
pp. 1084-1089 ◽  
Author(s):  
S. St-Pierre ◽  
P. Gaudreau ◽  
J. N. Drouin ◽  
D. Regoli ◽  
S. Lemaire
Keyword(s):  
Solid Phase ◽  
Gel Filtration ◽  
Rabbit Aorta ◽  
Paper Electrophoresis ◽  
Exchange Chromatography ◽  
Phase Method ◽  
Biological Assays ◽  
Structure Activity ◽  
Solid Phase Method ◽  
First Time

We have synthesized a series of 19 analogs of the octapeptide fragment of bradykinin (BK), des-Arg9-bradykinin, in order to perform a structure–activity study of this peptide on the newly discovered B1 receptor of bradykinin. The first time, each residue of the octapeptide was replaced by L-alanine to pinpoint biologically important residues. Thereafter, both phenylalanine residues in positions 5 and 8 were substituted by L-tyrosine methyl ether, L-cyclohexylalanine, D-phenylalanine, and L-leucine. This paper describes the synthesis of the analogs by the solid phase method. A Beckman peptide synthesizer was used to assemble the peptides on the resin support. Couplings were performed by the symmetrical anhydride procedure. After cleavage with liquid HF, the peptides were purified by ion-exchange chromatography on carboxymethylcellulose and by gel filtration on Bio-Gel P2 resin. The purity of the octapeptides was then checked by tlc, paper electrophoresis, amino acid analysis, and elemental analysis.The new peptides were tested on the rabbit aorta in order to evaluate their kinin-like activities and to see if they act as antagonists. The results of the biological assays are discussed in terms of structure–activity relationships.

Peculiarities of a solid-phase method for the Al-Fe/SiO2 and Al-Co/SiO2 powder catalysts production

2019 ◽  
pp. 63-68
Author(s):  
V.A. Artyukh ◽  
◽  
V.N. Borsch ◽  
V.S. Yusupov ◽  
S.Ya. Zhuk ◽  
...  
Keyword(s):  
Solid Phase ◽  
Phase Method ◽  
Solid Phase Method ◽  
Sio2 Powder
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