New analogs of arginine-vasopressin containing β-homo-L-amino acid residues

1989 ◽  
Vol 54 (10) ◽  
pp. 2795-2801 ◽  
Author(s):  
Krysztof Bankowski ◽  
Alexandra Misicka ◽  
Tomislav Barth ◽  
Jiřina Slaninová
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Arginine Vasopressin ◽  
Solid Phase ◽  
Phase Method ◽  
Amino Acid Residues ◽  
Solid Phase Method

Four new analogs of arginine vasopressin containing β-homo-L-amino acid residue were synthesized by the solid-phase method. The introduced modifications yielded the following peptides:[β-homo Phe3]AVP (I), [β-homoPro7]AVP (II), [Cpp1, Tyr(Me)2, β-homoPhe3]AVP (III), and[Cpp1,Tyr(Me)2, β-homoPro7]AVP (IV). Agonistic properties of I and II, as well as antagonistic properties of III and IV were decreased, more pronouncedly with analogs substituted in the position 3.

Synthesis of four new V1 antagonists of arginine-vasopressin (AVP) containing new thioacids at position 1 and their vasoconstrictor activity towards isolated mesenteric arterial vessels of rats

1991 ◽  
Vol 56 (2) ◽  
pp. 491-498 ◽  
Author(s):  
Bernard Lammek ◽  
Izabela Derdowska ◽  
Tomasz M. Wierzba ◽  
Witold Juzwa
Keyword(s):  
Peptide Synthesis ◽  
Arginine Vasopressin ◽  
Solid Phase ◽  
Structural Features ◽  
Phase Method ◽  
Competitive Antagonist ◽  
Vasoconstrictor Effect ◽  
Solid Phase Method

In an attempt to determine some of the structural features in position 1 that account for V1 antagonism, four new analogues of arginine-vasopressin were synthesized and the effect of the modifications on the vasoconstrictor activity was checked using isolated mesenteric arterial vessels of rats. The protected precursors required for these analogues were synthesized by a solid phase method of peptide synthesis. One of the reported analogues, namely [1-(4-mercapto-4-tetrahydrothiopyraneacetic acid)., 2-O-methyltyrosine, 8-arginine]vasopressin appears to be a potent competitive antagonist of the vasoconstrictor effect by AVP.

Synthesis of Tritium Labelled [8-Arginine]-vasopressin

1973 ◽  
Vol 51 (12) ◽  
pp. 1910-1914 ◽  
Author(s):  
H. Hutch Holton ◽  
Luis A. Branda ◽  
Barbara M. Ferrier
Keyword(s):  
Arginine Vasopressin ◽  
Solid Phase ◽  
Biological Activities ◽  
Phase Method ◽  
Natural Hormone ◽  
Solid Phase Method

Ring tritiated phenylalanine has been incorporated into [8-arginine]-vasopressin synthesized by the solid phase method. The peptide produced has levels of biological activities in agreement with those of the highly purified natural hormone.

Site Directed Antisera to the D-2 Polypeptide Subunit of Photosystem II

1987 ◽  
Vol 42 (4) ◽  
pp. 491-498 ◽  
Author(s):  
R. Geiger ◽  
R. J. Berzborn ◽  
B. Depka ◽  
W. Oettmeier ◽  
A. Trebst
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Photosystem Ii ◽  
Amino Acid Sequence ◽  
Solid Phase ◽  
High Titer ◽  
Membrane Surface ◽  
High Sensitivity ◽  
Phase Method ◽  
Solid Phase Method

Three synthetic oligopeptides were used for preparation of antibodies against the D-2 polypeptide of thylakoid membranes. Their sequence was chosen from a model of the folding of the amino acid sequence of the D-2 polypeptide subunit through the membrane that predicted these sequences to be exposed at the membrane surface. For the Merrifield solid-phase method on a fully automated synthesizer the Na-amino group was protected by a fluorenyl-9-methylcarbonyl group. The oligopeptides were coupled to serum albumin by EDAC for immunizations in rabbits. Antisera with high titer were obtained for the two oligopeptides that contained the amino acid sequence of the D-2 protein from amino acid 230 to 235 and from 235 to 241. The antisera reacted with the D-2 polypeptide, separated on SDS gel and agglutinated the thylakoid membrane. It is known that certain photosystem II functions are impaired by short time trypsin treatment of the membrane. The antisera were used to show that under these conditions the D-2 polypeptide in the membrane is very sensitive. The trypsination yielded two cleavage products detected by the two antisera, a 20 kDa fragment blotted by antiserum against amino acids 230 to 235 and a 10 kDa fragment blotted by the antiserum against amino acids 235 to 241. As the polypeptide cleavage occurs between the two epitopes, the trypsin cut is therefore at arginine 234. This supports the prediction that the sequence containing this arginine is the most exposed part of the D-2 polypeptide on the membrane (matrix) surface. It is proposed that the high sensitivity of the D-2 polypeptide accounts for the known effect of membrane trypsination on QA accessibility in photosystem II.

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.

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

Oxytocin analogues with non-coded amino acid residues in position 8: [8-Neopentylglycine]oxytocin and [8-cycloleucine]oxytocin

1987 ◽  
Vol 52 (9) ◽  
pp. 2317-2325 ◽  
Author(s):  
Jan Hlaváček ◽  
Jan Pospíšek ◽  
Jiřina Slaninová ◽  
Walter Y. Chan ◽  
Victor J. Hruby
Keyword(s):  
Amino Acid ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
The Other ◽  
Amino Acid Residues ◽  
Phase Synthesis ◽  
Other Hand ◽  
Fragment Condensation

[8-Neopentylglycine]oxytocin (II) and [8-cycloleucine]oxytocin (III) were prepared by a combination of solid-phase synthesis and fragment condensation. Both analogues exhibited decreased uterotonic potency in vitro, each being about 15-30% that of oxytocin. Analogue II also displayed similarly decreased uterotonic potency in vivo and galactogogic potency. On the other hand, analogue III exhibited almost the same potency as oxytocin in the uterotonic assay in vivo and in the galactogogic assay.

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 of a 21-Residue Fragment of Human Proinsulin by the Polyamide Solid Phase Method

1981 ◽  
Vol 362 (2) ◽  
pp. 833-840 ◽  
Author(s):  
Eric ATHERTON ◽  
Willy HÜBSCHER ◽  
Robert C. SHEPPARD ◽  
Vivienne WOOLLEY
Keyword(s):  
Solid Phase ◽  
Phase Method ◽  
Human Proinsulin ◽  
Solid Phase Method

scholarly journals Effect of roasting temperature on lipid and protein oxidation and amino acid residue side chain modification of beef patties

RSC Advances ◽  
2021 ◽  
Vol 11 (35) ◽  
pp. 21629-21641
Author(s):  
Chao Xia ◽  
Pingping Wen ◽  
Yaming Yuan ◽  
Xiaofan Yu ◽  
Yijing Chen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Protein Oxidation ◽  
Relative Number ◽  
Side Chain ◽  
Amino Acid Residues ◽  
Beef Patties ◽  
Lipid And Protein Oxidation ◽  
Roasting Temperature

The relative number of peptides modified by the amino acid residues of actin from raw beef patties and those cooked at different roasting temperatures.

scholarly journals Syntheses of two deacetyl-thymosin β4analogs and their anti-inflammatory effect on carrageenin-induced edema in the mouse paw

2001 ◽  
Vol 10 (2) ◽  
pp. 89-92 ◽  
Author(s):  
T. Abiko ◽  
R. Ogawa
Keyword(s):  
Marked Reduction ◽  
Solid Phase ◽  
The Other ◽  
Para Position ◽  
Phase Method ◽  
Antiinflammatory Effect ◽  
Solid Phase Method ◽  
Anti Inflammatory ◽  
Inflammatory Effect

Two {Met(0)6}deacetyl-thymosin β4analogs containing Phe(4F) or Tyr(Me) at position 12 were synthesized by the manual solid-phase method, and their anti-inflammatory effect on carrageenin-induced edema in the mouse paw was studied. Fluorination of the para-position of Phe12resulted in a marked antiinflammatory effect on carrageenin-induced edema in the mouse paw compared with that of our synthetic {Met(0)6}deacetyl-thymosin β4, but the other analog, {Met(0)6, Tyr(Me)12}deacetyl-thymosin β4, showed a marked reduction of the anti-inflammatory effect.

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