Semisynthetic synthesis and biological activity of a Clostridial-type ferredoxin free of aromatic amino acid residues

1974 ◽  
Vol 61 (1) ◽  
pp. 163-169 ◽  
Author(s):  
Eglis T. Lode ◽  
Cheryl L. Murray ◽  
Jesse C. Rabinowitz
1988 ◽  
Vol 53 (11) ◽  
pp. 2583-2590 ◽  
Author(s):  
Aleksandra Kubik ◽  
Zbigniew Szewczuk ◽  
Ignacy Z. Siemion ◽  
Zbigniew Wieczorek ◽  
Krystyna Spiegel ◽  
...  

The three analogues with D-amino acid substituents at position 1 and 5 of PRP-hexapeptide were synthesized and tested for its biological activity to check the influence of the spacial orientation of aromatic rings on the immune response. One of the analogs (Tyr-Val-Pro-Leu-D-Phe-Pro) was found to have the immunoregulatory activity.


1999 ◽  
Vol 64 (8) ◽  
pp. 1211-1252 ◽  
Author(s):  
Jan Hlaváček ◽  
Renáta Marcová

The first part of this review deals with the biosynthesis and a biological function of strongly vasoactive peptides named endothelins (ETs) including vasoactive intestinal contractor. Where it was useful, snake venoms sarafotoxins which are structural endothelin derivatives, were also mentioned. In the second part, an attention is paid to structural basis of the ETs biological activity, with respect to alterations of amino acid residues in the parent peptides modifying the conformation and consequently the physico-chemical and biological properties in corresponding ETs analogs. Special attention is focussed on the area of ETs receptors and their interaction with peptide and non peptide agonists and antagonists, important in designing selective inhibitors of ETs receptors potentially applicable as drugs in a medicine. A review with 182 references.


1984 ◽  
Vol 4 (12) ◽  
pp. 1009-1015 ◽  
Author(s):  
J. P. Bali ◽  
H. Mattras ◽  
A. Previero ◽  
M. A. Coletti-Previero

Rat blood was shown to contain an aminopeptidase which rapidly hydrolyses short peptides containing an aromatic amino acid as N-terminal residue. Using tetragastrin (Trp-Met-Asp-PheNH 2) as substrate, we showed that some amino acid hydroxamates inhibit rat aminopeptidase activity ‘in vitro’ in the following order: HTrpNHOH > HPheNHOH ≫ HAIaNHOH. The same hydroxamates markedly enhanced the biological activity of tetragastrin ‘in vivo’. The amplification of the secretory effect, correlated with the amount of the hydroxamate used, strongly suggests that these compounds can stabilize a number of active peptides in vivo by inhibiting their proteolytic degradation.


1990 ◽  
Vol 14 (1) ◽  
pp. 61-70 ◽  
Author(s):  
V.A. Lee ◽  
R.I. Musin ◽  
R.I. Tashmukhamedov ◽  
M.I. Shtilman ◽  
S.Sh. Rashidova

2019 ◽  
Vol 25 (69) ◽  
pp. 15779-15785 ◽  
Author(s):  
Kheironnesae Rahimidashaghoul ◽  
Iveta Klimánková ◽  
Martin Hubálek ◽  
Michal Korecký ◽  
Matúš Chvojka ◽  
...  

2019 ◽  
Vol 16 (11) ◽  
Author(s):  
Wojciech Lipinski ◽  
Joanna Wasko ◽  
Malgorzata Walczak ◽  
Justyna Fraczyk ◽  
Zbigniew J. Kaminski ◽  
...  

Biochemistry ◽  
1997 ◽  
Vol 36 (14) ◽  
pp. 4352-4359 ◽  
Author(s):  
Osamu Oishi ◽  
Shoji Yamashita ◽  
Etsuko Nishimoto ◽  
Sannamu Lee ◽  
Gohsuke Sugihara ◽  
...  

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