Analogs of arginine vasopressin modified in theN-terminal part of the molecule with a conformationally constrainedcis-peptide bond motif

2007 ◽  
Vol 13 (2) ◽  
pp. 128-132 ◽  
Author(s):  
Dariusz Sobolewski ◽  
Adam Prahl ◽  
Izabela Derdowska ◽  
Jiřina Slaninová ◽  
Krzysztof Kaczmarek ◽  
...  
2006 ◽  
Vol 49 (6) ◽  
pp. 2016-2021 ◽  
Author(s):  
Wioleta Kowalczyk ◽  
Adam Prahl ◽  
Izabela Derdowska ◽  
Dariusz Sobolewski ◽  
Jadwiga Olejnik ◽  
...  

2007 ◽  
Vol 50 (12) ◽  
pp. 2926-2929 ◽  
Author(s):  
Wioleta Kowalczyk ◽  
Dariusz Sobolewski ◽  
Adam Prahl ◽  
Izabela Derdowska ◽  
Lenka Borovičková ◽  
...  

1993 ◽  
Vol 58 (12) ◽  
pp. 2994-2999 ◽  
Author(s):  
Ewa Konieczna ◽  
Malgorzata Czaja ◽  
Bernard Lammek ◽  
Jiřina Slaninová ◽  
Tomislav Barth

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.


Author(s):  
Lenka Klasová ◽  
Štefan Zorad ◽  
Jiří Velek ◽  
Jan Ježek ◽  
Václav Kašička ◽  
...  

2005 ◽  
Vol 65 (4) ◽  
pp. 465-471
Author(s):  
D. Sobolewski ◽  
W. Kowalczyk ◽  
A. Prahl ◽  
I. Derdowska ◽  
J. Slaninova ◽  
...  

2008 ◽  
Vol 15 (3) ◽  
pp. 161-165 ◽  
Author(s):  
Dariusz Sobolewski ◽  
Adam Prahl ◽  
Anna Kwiatkowska ◽  
Jiřina Slaninová ◽  
Bernard Lammek
Keyword(s):  

1979 ◽  
Vol 44 (8) ◽  
pp. 2451-2454
Author(s):  
Anastasia Dimeli ◽  
Tomislav Barth

Vasopressin analogues containing an amino acid with a shorter side chain in position 8 of the peptide chain were more resistant to tryptic splitting of the peptide bond formed by the basic amino acid and terminal glycine amide. In the lysine vasopressin series, analogues with ornithine or lower homologues of lysine in position 8 were not hydrolyzed. In the arginine vasopressin series, the analogue containing 3-guanidino-2-aminopropionic acid in position 8 was completely resistant to the action of trypsin. The vasopressin analogue with norarginine in position 8 was split at a lower rate than natural arginine vasopressin.


2004 ◽  
Vol 63 (5) ◽  
pp. 420-425 ◽  
Author(s):  
W. Kowalczyk ◽  
I. Derdowska ◽  
O. Dawidowska ◽  
A. Prahl ◽  
B. Hartrodt ◽  
...  

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