Regina Kasprzykowska

The probable conformations of two cyclic enkephalin analogs, DNS-cyclo[D-Dab-Gly-Trp-Leu] (I) and... more The probable conformations of two cyclic enkephalin analogs, DNS-cyclo[D-Dab-Gly-Trp-Leu] (I) and DNScyclo[D-Dab-Gly-Trp-D-Leu] (II) (DNS = dansyl), were determined by combining the results of NOE, vicinal coupling constant and fluorescence energy transfer measurements with theoretical calculations. The common feature of the conformations for both peptides is the presence of a/~-turn at residues 2 and 3.

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Development of vasopressor specific vasotocin analogues with prolonged effects

Peptides 1990, 1991

Simple and efficient synthesis of chiral amino alcohols with an amino acid-based skeleton

Letters in Peptide Science, 2003

Sodium bis(2-methoxyethoxy)aluminum hydride, NaA1H2(OCH2CH2OCH3)2, commercially known as Vitride ... more Sodium bis(2-methoxyethoxy)aluminum hydride, NaA1H2(OCH2CH2OCH3)2, commercially known as Vitride | or Red-A1 | enables rapid synthesis of pure optically active N-protected amino alcohols and peptide alcohols in very high yields. The method is very simple and attractive, as it does not require an additional step of N-protected amino acid derivatization and proceeds without the loss of enantiomeric homogeneity.

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Oxidation of L-lysine derivatives to L-α-aminoadipamic acid (homoglutamine) derivatives with KMnO 4

International Journal of Peptide and Protein Research, 1987

Side reactions of monoaminodicarboxylic acids in peptide synthesis

International Journal of Peptide and Protein Research, 1988

ChemInform Abstract: Thermal Dehydration of Polyhydroxy Alcohols. Part 1. The Solvent-Free Thermal Dehydration of Tetritols on Zeolites

ChemInform, 2000

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Conformation-activity study of the uterotonic antagonists of oxytocin

Peptides 1992, 1993

Cystatin C Based Peptidyl Diazomethanes as Cysteine Proteinase Inhibitors: Influence of the Peptidyl Chain Length

Journal of Enzyme Inhibition and Medicinal Chemistry, 1992

The peptidyl diazomethanes Cbz-Gly-CHN2, Boc-Val-Gly-CHN2, H-Leu-Val-Gly-CHN2, Cbz-Leu-Val-Gly-CH... more The peptidyl diazomethanes Cbz-Gly-CHN2, Boc-Val-Gly-CHN2, H-Leu-Val-Gly-CHN2, Cbz-Leu-Val-Gly-CHN2 and Cbz-Arg-Leu-Val-Gly-CHN2, with peptidyl portions modelled after the proposed cysteine proteinase interacting N-terminal segment of human cystatin C, were synthesized. Their efficiency as cysteine proteinase inhibitors was tested against papain, human cathepsin B and bovine cathepsin B. All, except Cbz-Gly-CHN2, were found to be irreversible inhibitors of the tested enzymes. Each addition of an amino acid residue to their peptidyl portions resulted in an increased inhibition rate of all three enzymes. These data suggest that the arginyl residue of the tetrapeptidyl diazomethane, and also the corresponding arginyl residue in native cystatin C, interact with a S4 substrate pocket subsite of both papain and cathepsin B. The most efficient inhibitor, Cbz-Arg-Leu-Val-Gly-CHN2, inhibited papain and cathepsin B with rate constants of the same order of magnitude as those for L-3-carboxy-trans-2,3-epoxypropionyl-leucylamido-(4-guanidin o)butane (E-64). The high water-solubility of Cbz-Arg-Leu-Val-Gly-CHN2 allowing it to be dissolved to molar concentrations without use of non-physiological additives, makes it suitable for in vitro and in vivo cysteine proteinase inhibition studies.

Efficient routes to the Arnstein's tripeptide δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine (LLD ACV) from the oxidation products of L-lysine derivatives

Collection of Czechoslovak Chemical Communications, 1988

Two efficient syntheses of the linear tripeptide precursor of penam and cephem antibiotics are pr... more Two efficient syntheses of the linear tripeptide precursor of penam and cephem antibiotics are presented. The routes are characterised by the use of L-lysine derivatives, Z-L-Lys(Z)-OH and H-L-Lys(Z)-OH as starting materials. By the permanganate oxidation the protected side chain amino grouping in L-lysine derivatives is transformed into the benzyloxycarbonylcarbamoyl substituent with formation of Z-L-Aad(NHZ)-OH and H-L-Aad(NHZ)-OH compounds. Both oxidation products are easily transformed into [N, Cα]-diprotected derivatives. Subsequent condensation at the δ-carboxy group afforded protected LLD ACV tripeptide.