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Substrate for carboxypeptidase Y from baker's yeast.

Functional Peptides
Catalog number
CAS number
Molecular Formula
Molecular Weight
Z-L-phenylalanyl-L-glycine; N-Carbobenzoxy-L-phenylalanylglycine; N-benzyloxycarbonylphenylalanylglycine; Z Phe Gly OH
White powder
≥ 99% (TLC)
Melting Point
148-152 °C
Boiling Point
669.9°C at 760 mmHg
Store at 2-8°C
InChI Key
Canonical SMILES
1. Z-Phe-Gly-NHO-Bz, an inhibitor of cysteine cathepsins, induces apoptosis in human cancer cells
D M Zhu, F M Uckun Clin Cancer Res. 2000 May;6(5):2064-9.
An increasing number of studies indicate that cysteine cathepsins contribute to cancer progression, invasion, and metastasis. Here we provide experimental evidence that the cathepsin inhibitor Z-Phe-Gly-NHO-Bz induces rapid apoptotic death in human cancer cell lines. Notably, the Z-Phe-Gly-NHO-Bz-induced apoptosis exhibited independence of p53, caspases, and mitogen-activated protein (MAP) kinases. Taken together, our results prompt the hypothesis that cysteine cathepsin(s) is a universal survival factor for cancer cells, and its inhibition leads to cancer cell apoptosis. The exquisite sensitivity of human cancer cells to CATI-1 indicates that this compound and its derivatives may provide the basis for new treatment programs against a broad spectrum of malignancies.
2. Phosphinic peptide analogues as potent inhibitors of Corynebacterium rathayii bacterial collagenase
A Yiotakis, A Lecoq, A Nicolaou, J Labadie, V Dive Biochem J. 1994 Oct 1;303 ( Pt 1)(Pt 1):323-7. doi: 10.1042/bj3030323.
Pseudo-substrate analogues of collagenase from Corynebacterium rathayii, in which the scissile peptide bond is replaced by a phosphinic moiety, were synthesized and evaluated as inhibitors of this enzyme. The phosphinic tetrapeptide, Z-Phe-psi(PO2CH2)-Gly-Pro-Nle (1), was found to be a potent inhibitor of collagenase with a Ki value of 8 nM. Increasing the length of the phosphinic-containing inhibitors from tetra- to hepta-peptide size further improves the potency of these compounds. The heptapeptide analogue, Z-Phe-Gly-Pro-Phe-psi(PO2CH2)-Gly-Pro-Nle-OMe, with a Ki value of 0.6 nM, is the most potent inhibitor reported to date for bacterial collagenases. A comparison between the phosphinic analogue Z-Phe-psi(PO2CH2)-Gly-Pro-Nle (1) and the phosphonamide peptide Z-Phe-psi(PO2NH)-Gly-Pro-Nle (2) shows that for bacterial collagenase the replacement of a CH2 by an NH group results only in a modest increase in affinity from Ki = 8 nM for compound 1 to Ki = 6 nM for compound 2. Most of the phosphorus-containing inhibitors of this series are slow- or slow-tight-binding inhibitors with second-order rate constants for association and dissociation varying respectively for the kon values from 1 x 10(3) to 26 x 10(3) M-1.s-1 and for the koff values from 3 x 10(-4) to 2 x 10(-5) s-1. Interestingly, the lower affinity of the molecule containing a D residue in the P1 position of the inhibitor, compared with the molecule with an L residue in this position, is mainly the consequence of a lower rate constant for association of these D stereoisomers with the enzyme. This study demonstrates that phosphinic peptide analogues are potent inhibitors of a bacterial collagenase. The development of new phosphinic peptides should lead to the discovery of potent inhibitors of other zinc metalloproteases. Details of how the analogues were synthesized are given in Supplementary Publication SUP 50176 (14 pages), which has been deposited with the British Library Document Supply Centre, Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, from whom copies can be obtained on the terms indicated in Biochem. J. (1994) 297, 9.
3. Effect of the ΔPhe residue configuration on a didehydropeptides conformation: A combined CD and NMR study
Marek Lisowski, Lukasz Jaremko, Mariusz Jaremko, Adam Mazur, Rafał Latajka, Maciej Makowski Biopolymers. 2010 Dec;93(12):1055-64. doi: 10.1002/bip.21522.
Conformations of two pairs of dehydropeptides with the opposite configuration of the ΔPhe residue, Boc-Gly-Δ(Z)Phe-Gly-Phe-OMe (Z-OMe), Boc-Gly-Δ(E)Phe-Gly-Phe-OMe (E-OMe), Boc-Gly-Δ(Z)Phe-Gly-Phe-p-NA (Z-p-NA), and Boc-Gly-Δ(E)Phe-Gly-Phe-p-NA (E-p-NA) were compared on the basis of CD and NMR studies in MeOH, trifluoroethanol (TFE), MeCN, chloroform, and dimethylsulfoxide (DMSO). The CD results were used as the additional input data for the NMR-based determination of the detailed solution conformations of the peptides. It was found that E-OMe is unordered and Z-OMe, Z-p-NA, and E-p-NA adopt the β-turn conformation. There are two overlapping β-turns in each of those peptides: type II and type III' in Z-OMe and Z-p-NA, and two type III in E-p-NA. The ordered structure-inducing properties of Δ(Z)Phe and Δ(E)Phe in the peptides studied depend on the C-terminal blocking group. In methyl esters, the Δ(Z)Phe residue is a strong inducer of ordered conformations whereas the Δ(E)Phe one has no such properties. In p-nitroanilides, both isomers of ΔPhe cause the peptides to adopt ordered structures to a similar extent.

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