Synthese eines Thymosin β10-Fragments zur Entwicklung spezifischer Antikörper / Synthesis of a Fragment of Thymosin β10 for the Development of Specific Antibodies

The N-terminal fragment 1-12 of thymosin β10 was synthesized by the solid phase method using p-benzyloxybenzyl alcohol/polystyrene/divinylbenzeneresin and N-a-Fmoc amino acids with tert-butyl or Boc side chain protecting groups. Coupling was performed with BOP. The peptide was purified by preparative HPLC.

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Synthese der vorgeschlagenen Sequenz für ein neues Thymosin aus Forellenmilz / Synthesis of a New Thymosine from Trout Spleen

Zeitschrift für Naturforschung B ◽

10.1515/znb-1990-1220 ◽

1990 ◽

Vol 45 (12) ◽

pp. 1725-1728

Author(s):

Wolfgang Voelter ◽

Hubert Kalbacher ◽

Hartmut Echner ◽

Bettina Schmid ◽

Udo Treffer ◽

...

Keyword(s):

Amino Acids ◽

Solid Phase ◽

Side Chain ◽

Phase Method ◽

Preparative Hplc ◽

Gel Chromatography ◽

Tert Butyl ◽

Solid Phase Method

Thymosine β11, a peptide structurally very similar to the known thymosine β11, was recently isolated from trout spleen and synthesized by the solid phase method using the p-benzyloxybenzyl alcohol/polystyrene/divinylbenzene resin, Nα-Fmoc-amino acids and those with tert-butyl or Boc side chain protection. All couplings are performed with the DCC reagent. The peptide is purified by a combination of gel chromatography and preparative HPLC.

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Synthesis and biological activity of new metallocenic angiotensin II analogs

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19882914 ◽

1988 ◽

Vol 53 (11) ◽

pp. 2914-2919 ◽

Cited By ~ 10

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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Solid-phase synthesis of peptide selenoesters via a side-chain anchoring strategy

Chemical Communications ◽

10.1039/c7cc00823f ◽

2017 ◽

Vol 53 (39) ◽

pp. 5424-5427 ◽

Cited By ~ 16

Author(s):

Cameron C. Hanna ◽

Sameer S. Kulkarni ◽

Emma E. Watson ◽

Bhavesh Premdjee ◽

Richard J. Payne

Keyword(s):

Solid Phase Synthesis ◽

Solid Phase ◽

Side Chain ◽

Phase Method ◽

Phase Synthesis ◽

Solid Phase Method

A robust, high yielding and epimerisation-free solid-phase method for accessing peptide selenoesters is reported.

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

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19941430 ◽

1994 ◽

Vol 59 (6) ◽

pp. 1430-1438 ◽

Cited By ~ 10

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.

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The Analogs of [D-Har8]Vasopressin with Di- and Trisubstituted Phenylalanine in Position 2; Synthesis and Some Biological Properties

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19932751 ◽

1993 ◽

Vol 58 (11) ◽

pp. 2751-2760 ◽

Cited By ~ 4

Author(s):

Miroslava Žertová ◽

Zdenko Procházka ◽

Jiřina Slaninová ◽

Tomislav Barth ◽

Pavel Majer ◽

...

Keyword(s):

Amino Acids ◽

Solid Phase ◽

Biological Properties ◽

Phase Method ◽

Antidiuretic Activity ◽

Solid Phase Method

Four analogs of vasopressin with non-coded amino acids D-homoarginine (in position 8) and 2,6-di- or 2,4,6-trisubstituted L- or D-phenylalanine (in position 2) were synthesized using the solid phase method on p-methylbenzhydrylamine resin. All the analogs were found to be uterotonic inhibitors, the most potent one in vitro and in vivo being [D-Phe(2,4,6-triMe)2,D-Har8]vasopressin with pA2 values equal to 8.1 and 7.5, respectively. All of them had negligible antidiuretic activity and were weak pressor inhibitors.

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A simple and traceless solid phase method simplifies the assembly of large peptides and the access to challenging proteins

Chemical Science ◽

10.1039/c7sc01912b ◽

2017 ◽

Vol 8 (8) ◽

pp. 5362-5370 ◽

Cited By ~ 14

Author(s):

N. Ollivier ◽

R. Desmet ◽

H. Drobecq ◽

A. Blanpain ◽

E. Boll ◽

...

Keyword(s):

Amino Acids ◽

Solid Phase ◽

Biologically Active ◽

Phase Method ◽

Active Protein ◽

Solid Phase Method

We show that the combination of solid phase and solution ligation techniques facilitates the production of a challenging and biologically active protein made of 180 amino acids.

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Amino Acids and Peptides. XXXV. Facile Preparation of p-Nitroanilide Analogs by the Solid-Phase Method.

Chemical and Pharmaceutical Bulletin ◽

10.1248/cpb.48.1740 ◽

2000 ◽

Vol 48 (11) ◽

pp. 1740-1744 ◽

Cited By ~ 21

Author(s):

Keiko HOJO ◽

Mitsuko MAEDA ◽

Shin IGUCHI ◽

Timothy SMITH ◽

Hiroshi OKAMOTO ◽

...

Keyword(s):

Amino Acids ◽

Solid Phase ◽

Phase Method ◽

Solid Phase Method ◽

Facile Preparation

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

Zeitschrift für Naturforschung C ◽

10.1515/znc-1987-0427 ◽

1987 ◽

Vol 42 (4) ◽

pp. 491-498 ◽

Cited By ~ 21

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.

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