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  • Title: Distance between the basic group of the amino acid residue's side chain in position P1 of trypsin inhibitor CMTI-III and Asp189 in the substrate pocket of trypsin has an essential influence on the inhibitory activity.
    Author: Jaśkiewicz A, Lesner A, Rózycki J, Rodziewicz S, Rolka K, Ragnarsson U, Kupryszewski G.
    Journal: Biochem Biophys Res Commun; 1997 Nov 26; 240(3):869-71. PubMed ID: 9398660.
    Abstract:
    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 with L-lysine residue in position P1 showed 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 P1 of the trypsin inhibitor CMTI-III and Asp189 in the substrate pocket of trypsin plays an essential role for the trypsin-inhibitor interaction.
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