Fibrous Aggregates of Short Peptides Containing Two Distinct Aromatic Amino Acid Residues

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

2020 ◽  
Vol 681 ◽  
pp. 108264
Author(s):  
Sandra Skibiszewska ◽  
Szymon Żaczek ◽  
Agnieszka Dybala-Defratyka ◽  
Katarzyna Jędrzejewska ◽  
Elżbieta Jankowska

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.


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

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

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