Synthesis and Some Pharmacological Properties of Six New Analogs of Arginine-Vasopressin Substituted in Position 2 with β-Thienylalanine or Prolonged on the N-Terminus with 1-Adamantaneacetic Acid

1993 ◽  
Vol 58 (12) ◽  
pp. 2994-2999 ◽  
Author(s):  
Ewa Konieczna ◽  
Malgorzata Czaja ◽  
Bernard Lammek ◽  
Jiřina Slaninová ◽  
Tomislav Barth
Keyword(s):  
Arginine Vasopressin ◽  
Peptide Bond ◽  
Pharmacological Properties ◽  
N Terminus

Six new analogs of arginine-vasopressin, four of them substituted in position 2 with β-thienylalanine and two prolonged on the n-terminus by acylation with 1-adamantaneacetic acid, were synthesized on chloromethylated resin using Boc strategy and DCC or DCC-HOBt to form peptide bond. The activity of the analogs was fairly low, however, one of the peptides, namely [Cpp1, Thi2, Val4]AVP, showed selectivity in antiuterotonic, antipressor and anti-antidiuretic effects.

Synthesis and some pharmacological properties of potent and selective antagonists of the vasopressor (V1-receptor) response to arginine-vasopressin

1992 ◽  
Vol 35 (2) ◽  
pp. 382-388 ◽  
Author(s):  
Maurice Manning ◽  
Stoytcho Stoev ◽  
Krzysztof Bankowski ◽  
Aleksandra Misicka ◽  
Bernard Lammek ◽  
...  
Keyword(s):  
Arginine Vasopressin ◽  
Pharmacological Properties ◽  
Receptor Response ◽  
Selective Antagonists

4-Phenylalanine analogues of vasopressin: Synthesis, pharmacological and chiroptical properties

1986 ◽  
Vol 51 (7) ◽  
pp. 1532-1541 ◽  
Author(s):  
František Brtník ◽  
Tomislav Barth ◽  
Petr Maloň ◽  
Ivo Frič ◽  
Vija E. Kluša ◽  
...  
Keyword(s):  
Arginine Vasopressin ◽  
Pharmacological Properties ◽  
Cd Spectra ◽  
Chiroptical Properties ◽  
Lysine Vasopressin ◽  
Vasopressin Synthesis

Synthesis, some pharmacological properties and CD spectra of [4-phenylalanine, 8-arginine]vasopressin and [4-phenylalanine, 8-lysine]vasopressin are described.

scholarly journals Maturation of IncP Pilin Precursors Resembles the Catalytic Dyad-Like Mechanism of Leader Peptidases

2000 ◽  
Vol 182 (23) ◽  
pp. 6751-6761 ◽  
Author(s):  
Ralf Eisenbrandt ◽  
Markus Kalkum ◽  
Rudi Lurz ◽  
Erich Lanka
Keyword(s):  
Amino Acid ◽  
Peptide Bond ◽  
Ring Structure ◽  
Site Directed Mutagenesis ◽  
Signal Peptidase ◽  
Ionization Mass ◽  
Preparation Technique ◽  
Core Sequence ◽  
Specific Phage ◽  
N Terminus

ABSTRACT The pilus subunit, the pilin, of conjugative IncP pili is encoded by the trbC gene. IncP pilin is composed of 78 amino acids forming a ring structure (R. Eisenbrandt, M. Kalkum, E.-M. Lai, C. I. Kado, and E. Lanka, J. Biol. Chem. 274:22548–22555, 1999). Three enzymes are involved in maturation of the pilin: LepB ofEscherichia coli for signal peptide removal and a yet-unidentified protease for removal of 27 C-terminal residues. Both enzymes are chromosome encoded. Finally, the inner membrane-associated IncP TraF replaces a four-amino-acid C-terminal peptide with the truncated N terminus, yielding the cyclic polypeptide. We refer to the latter process as “prepilin cyclization.” We have used site-directed mutagenesis of trbC and traF to unravel the pilin maturation process. Each of the mutants was analyzed for its phenotypes of prepilin cyclization, pilus formation, donor-specific phage adsorption, and conjugative DNA transfer abilities. Effective prepilin cyclization was determined by matrix-assisted laser desorption-ionization–mass spectrometry using an optimized sample preparation technique of whole cells and trans-3-indolyl acrylic acid as a matrix. We found that several amino acid exchanges in the TrbC core sequence allow prepilin cyclization but disable the succeeding pilus assembly. We propose a mechanism explaining how the signal peptidase homologue TraF attacks a C-terminal section of the TrbC core sequence via an activated serine residue. Rather than cleaving and releasing hydrolyzed peptides, TraF presumably reacts as a peptidyl transferase, involving the N terminus of TrbC in the aminolysis of a postulated TraF-acetyl-TrbC intermediate. Under formal loss of a C-terminal tetrapeptide, a new peptide bond is formed in a concerted action, connecting serine 37 with glycine 114 of TrbC.

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