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4 Polish Journal of Chemistry

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New Analogues of Cucurbita maxima Trypsin Inhibitor III (CMTI-III) Substituted with D-Arg or D-Lys in Position 5 (P1)

Frąszczak P., Rolka K., Kupryszewski G.

Polish Journal of Chemistry

2002

Vol. 76 / nr 4

519-523

Two new analogues of trypsin inhibitor CMTI-III substituted with D-Arg or D-Lys in position 5 (P1) were synthesized by the solid-phase method. The first analogue ([D-Arg5] CMTI-III) displayed association equilibrium constants (Ka) with bovine -trypsin by about three orders of magnitude lower than did wild CMTI-III. The second analogue ([D-Lys5] CMTI-III) displayed Ka by about four orders of magnitude lower than [Lys5] CMTI-III. The configuration of basic amino acid residue (Arg or Lys) in the reactive site (position P1) of CMTI-III and its analogues played an important role for the stabilization of the inhibitors active structure.

Low Molecular Mass Inhibitors of Bovine beta-Trypsin Containing Binding Loop Fragment of CMTI-III. Synthesis and Evaluation of Inhibitory Activity

Frąszczak P., Lis K., Jaśkiewicz A., Miecznikowska H., Rolka K., Kupryszewski G.

Polish Journal of Chemistry

2001

Vol. 75, nr 12

1863-1868

Three peptides with sequences related to the binding loop of Cucurbita maxima trypsin inhibitor III were obtained: [G3,GIO]CMTI-HI (1-10) (1), [A1,G3,A9,G10]MTlII (1-10) (2) and c(K-A-A-P-R-I-L-M-K-Y-A-E) (3). All peptides were synthesized by the solid-phase methodusing the Fmoc/Bu t procedure. Peptide 1 revealed a relatively high inhibitory activity (association equilibrium constant with bovine beta-trypsin Ka = 4 x 10 9 [M -1]). Significantly lower activity (Ka = 3.6x l O4 [M -1) was obtained for peptide 3. Peptide 2 appeared to be inactive.

Synthesis of Hepatitis C Virus Protein Fragments and Evaluation of Their Immunogenicity : Part II

Klugmann K., Karawajczyk B., Kunikowska D., Głosnicka R., Maćkiewicz A.

Polish Journal of Chemistry

2000

Vol. 74, nr 8

1085-1090

Three polypetide fragments of hepatitis C virus protein were synthesized using the solid-phase method. The immunogenicity of the peptides was tested. All the peptides exhibit immunological activity.

Synthesis of hepatitic C virus protein fragments and evaluation of their immunogenicity

Karawajczyk B., Maćkiewicz Z., Kunikowska D., Dziadziuszko H., Dera-Tomaszewska B., Głośnicka R., Kupryszewski G.

Polish Journal of Chemistry

1998

Vol. 72, nr 1

84-88

Three polypeptide fragments of Hepatitis C virus protein (130-140)C, (133-142)C and (1406-1415)NS3 were synthesized using the solid-phase method. The immunogenicity of the peptides was tested on rabbits. All the peptides studied revealed homoral and cell response.