New method for the synthesis of N-methyl amino acids containing peptides by reductive methylation of amino groups on the solid phase

2009 ◽  
Vol 42 (2) ◽  
pp. 118-124 ◽  
Author(s):  
KALLE KALJUSTE ◽  
ANDERS UNDÉN
Keyword(s):  
Amino Acids ◽  
Solid Phase ◽  
New Method ◽  
Amino Groups ◽  
Reductive Methylation

A new method of quaternizing amines and its use in amino acid and peptide chemistry

1976 ◽  
Vol 54 (20) ◽  
pp. 3310-3311 ◽  
Author(s):  
Francis C. M. Chen ◽  
N. Leo Benoiton
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Methyl Iodide ◽  
New Method ◽  
Hydroxyl Groups ◽  
Amino Groups ◽  
Small Peptides ◽  
Peptide Chemistry ◽  
Selective Reagent ◽  
Derivatives Of

Methyl iodide and potassium bicarbonate in methanol is presented as a mild, efficient, and selective reagent for the quaternization of amino groups. It does not attack hydroxyl groups. Its use with amino acids, derivatives of lysine, and small peptides is described.

Two different approaches for developing immunometric assays of haptens

1996 ◽  
Vol 42 (9) ◽  
pp. 1532-1536 ◽  
Author(s):  
J Grassi ◽  
C Créminon ◽  
Y Frobert ◽  
E Etienne ◽  
E Ezan ◽  
...  
Keyword(s):  
Amino Acids ◽  
Monoclonal Antibody ◽  
Solid Phase ◽  
Leukotriene C4 ◽  
Amino Groups ◽  
Small Peptides ◽  
Assay Sensitivity ◽  
Primary Amino ◽  
C And N

Abstract To improve immunoassays of small haptens, we developed two different approaches for their measurement in a non-competitive format. We first devised two-site immunometric assays for small peptides (8-11 amino acids) by selecting two sets of antibodies specifically directed against C- and N-terminal moieties of the peptides. In each case, assay sensitivity improved substantially over that of the corresponding competitive assays. More interestingly, all of these new immunometric assays were much more specific than the competitive assays. In a second approach, we developed a new procedure, solid-phase-immobilized epitope immunoassay (SPIE-IA), in which a single monoclonal antibody uses the same epitope for capture and tracer binding and the hapten is covalently cross-linked to solid-phase proteins. To date, SPIE-IA have been successfully applied to the determination of haptens bearing primary amino groups, including substance P, thyroxine, leukotriene C4, endothelin, and angiotensin II. In each case, assay sensitivity was significantly improved.

Solid Phase Synthesis of Thymopoietin-(32-36) Using Adpoc Amino Acids and its Biological Activity +

1980 ◽  
Vol 35 (11) ◽  
pp. 1476-1478 ◽  
Author(s):  
Georg Rampold ◽  
Elsa Lundanes ◽  
Karl Folkers ◽  
Wolfgang Voelter ◽  
Hubert Kalbacher ◽  
...  
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Antibody Level ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Model System ◽  
Amino Groups ◽  
Phase Synthesis ◽  
First Time ◽  
Low Activity

Abstract An exemplary peptide has been synthesized for the first time by an automated solid-phase instrumentation which utilized the new Adpoc (1 -(1-adamantyl) -1 -methylethoxycarbonyl-) group for protection of the a-amino groups of the amino acids. The pentapeptide, thymo-poietin-(32-36) was synthesized, and shown to be pure by criteria including HPLC. Using a Cytoxan (cyclophosphamide) model system for suppression of a primary, hemolytic, humoral, antibody level, thymopoietin-(32-36) showed low activity, and reversed the suppressing effect of Cytoxan. This biological activity apparently is the result of cummulative effect.

Vasopressin and oxytocin analogs with interchanged sequence of amino acids in positions 7 and 8. synthesis and biological effects

1981 ◽  
Vol 46 (9) ◽  
pp. 2136-2139 ◽  
Author(s):  
Ivo Bláha ◽  
Viktor Krchňák ◽  
Milan Zaoral
Keyword(s):  
Amino Acids ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Biological Effects ◽  
Free Flow ◽  
Protecting Groups ◽  
Pressor Effect ◽  
Phase Synthesis ◽  
Antidiuretic Effect

p-Toluenesulfonyl-S-benzylcysteinyl-tyrosyl-phenylalanyl-glutaminyl-asparaginyl-S-benzylcysteinyl-NG-p-toluenesulfanylarginyl-prolyl-glycineamide (I) and S-benzylcysteinyl-tyrosyl-isoleucyl-glutaminyl-asparaginyl-S-benzylcysteinyl-leucyl-prolyl-glycine amide (III) were prepared by solid phase synthesis. After removal of the protecting groups, closure of the disulfide ring, and purification by continuous free-flow electrophoresis [arginine7, proline8]vasopressin (II) and [leucine7, proline8]oxytocin (IV) were obtained. The antidiuretic effect of II is markedly higher than its pressor effect; IV possesses c. 6% of the uterotonic and c. 10% of the galactogogous effect of oxytocin.

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.

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