| Autor: |
Jaśkiewicz, Anna, Lesner, Adam, Różycki, Jan, Rodziewicz, Sylwia, Rolka, Krzysztof, Ragnarsson, Ulf, Kupryszewski, Gotfryd |
| Zdroj: |
Biochemical and Biophysical Research Communications; November 1997, Vol. 240 Issue: 3 p869-871, 3p |
| Abstrakt: |
Three new analogues of trypsin inhibitor CMTI-III were synthesized by the solid-phase method: [Lys5]CMTI-III, [Orn5]CMTI-III and [Dab5]CMTI-III. Only one analogue withl-lysine residue in position P1showed inhibitory activity of the same order of magnitude as did wild CMTI-III. Two remaining analogues were completely inactive. A conclusion was drawn that the distance between the basic group of the amino acid residue's side chain in position P1of the trypsin inhibitor CMTI-III and Asp189in the substrate pocket of trypsin plays an essential role for the trypsin–inhibitor interaction. |
| Databáze: |
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