| Autor: |
Marchenko AV, Stepanova EO, Sekridova AV, Sidorova MV, Bushuev VN, Bespalova ZhD, Shirinskiĭ VP |
| Jazyk: |
ruština |
| Zdroj: |
Biofizika [Biofizika] 2010 Nov-Dec; Vol. 55 (6), pp. 1008-13. |
| Abstrakt: |
The ability of novel cell-permeating peptide molecules derived from the peptide inhibitor of the myosin light chain kinase (MLCK) L-PIK (Arg-Lys-Lys-Tyr-Lys-Tyr-Arg-Arg-Lys) to inhibit this kinase in vitro and attenuate the thrombin-induced hyperpermeability of endothelial cell monolayer in culture has been studied. It was found that the compounds [NalphaMeArg1]-L-PIK and [Cit1]-L-PIK possess the inhibitory activity towards MLCK comparable to that of L-PIK and the ability to suppress the hyperpermeability of endothelium, whereas other modifications of L-PIK were less effective. Thus, among de novo synthesized peptides, [NalphaMeArg1]-L-PIK and [Cit1]-L-PIK demonstrate the inhibitory properties of the original peptide L-PIK and additionally surpass it by stability in blood plasma. These peptides may be used in the design of novel antiedemic drugs. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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