Studies on α_2-Plasmin Inhibitor Fragment T-11. III. Structure-Activity Relationships among the Fragments of T-11, the Plasminogen Binding Site(s) of Human α_2-Plasmin Inhibitor(Medicinal Chemistry,Chemical)

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Twelve shortened fragments of peptide T-11, which is a part of human α_2-plasmin inhibitor and contains its plasmin(ogen)-binding site(s) were synthesized by a conventional solution method. The dissociation constants for the interaction between these synthetic fragments and plasmin were determined. Among these fragments, the octadecapep tide containing C-terminal lysine of T-11, which consists of 26 amino acids, was found to be the smallest active fragment of T-11. The N-terminal and the central portion fragments of T-11 possessed no binding activity. The heptadecapeptide which has the same sequence as the octadecapeptide but lacks the C-terminal lysine showed no binding activity. The hexadecapeptide containing the C-terminal lysine but lacking the 10th lysine in T-11 scarcely exhibited the activity. Thus, the lysine residues at positions 10 and 26 in T-11 must be important for the activity.
公益社団法人日本薬学会の論文
1987-07-25