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Substrate for carboxypeptidase Y.

Functional Peptides
Catalog number
CAS number
Molecular Formula
Molecular Weight
(2S)-4-methyl-2-[[(2S)-3-phenyl-2-(phenylmethoxycarbonylamino)propanoyl]amino]pentanoic acid
Z-L-phenylalanyl-L-leucine; (S)-2-((S)-2-(benzyloxycarbonylamino)-3-phenylpropanamido)-4-methylpentanoic acid; Z Phe Leu OH
White powder
≥ 98% (HPLC)
Boiling Point
674.4°C at 760 mmHg
Store at -20 °C
InChI Key
Canonical SMILES
1. C- and N-terminal residue effect on peptide derivatives' antagonism toward the formyl-peptide receptor
Alessandro Dalpiaz, Maria E Ferretti, Gianni Vertuani, Serena Traniello, Angelo Scatturin, Susanna Spisani Eur J Pharmacol. 2002 Feb 2;436(3):187-96. doi: 10.1016/s0014-2999(01)01627-2.
The biological action of several X-Phe-D-Leu-Phe-D-Leu-Z (X=3',5'-dimethylphenyl-ureido; Z=Phe, Lys, Glu, Tyr) analogues was analysed on human neutrophils to evaluate their ability to antagonize formyl-peptide receptors. X-Phe-D-Leu-Phe-D-Leu-Phe analogues obtained as C-terminal olo or amido derivatives and T-Phe-D-Leu-Phe-D-Leu-Phe analogues (T=thiazolyl-ureido) were also analysed. The activities of pentapeptide derivatives were compared with those of X-Phe-D-Leu-Phe-D-Leu-Phe chosen as reference antagonist. Our results demonstrate that X-Phe-D-Leu-Phe-D-Leu-Phe-olo, X-Phe-D-Leu-Phe-D-Leu-Glu and X-Phe-D-Leu-Phe-D-Leu-Tyr are more active antagonists than X-Phe-D-Leu-Phe-D-Leu-Phe. The presence of Lys (X-Phe-D-Leu-Phe-D-Leu-Lys) seems, instead, to inhibit the formyl-peptide receptor antagonist properties. The presence of the N-terminal thiazolyl-ureido group seems to considerably contribute to the receptor antagonist properties of T-Phe-D-Leu-Phe-D-Leu-Phe-OH. The introduction of the C-terminal methyl ester (T-Phe-D-Leu-Phe-D-Leu-Phe-OMe) or amido group (X-Phe-D-Leu-Phe-D-Leu-Phe-NH2) appears detrimental for the affinity and formyl-peptide receptor antagonist properties of the Phe-D-Leu-Phe-D-Leu-Phe derivatives. The examined peptides inhibit superoxide anion production and lysozyme release more efficaciously than neutrophil chemotaxis.
2. Conformations of dehydrophenylalanine containing peptides. Nuclear Overhauser effect study of two acyclic tetrapeptides
K Uma, V S Chauhan, A Kumar, P Balaram Int J Pept Protein Res. 1988 Apr;31(4):349-58. doi: 10.1111/j.1399-3011.1988.tb00044.x.
Two isomeric, acyclic tetrapeptides containing a Z-dehydrophenylalanine residue (delta Z-Phe) at position 2 or 3, Boc-Leu-Ala-delta Z-Phe-Leu-OMe (1) and Boc-Leu-delta Z-Phe-Ala-Leu-OMe (2), have been synthesized and their solution conformations investigated by 270 MHz 1H n.m.r. spectroscopy. In peptide 1 the Leu(4) NH group appears to be partially shielded from solvent, while in peptide 2 both Ala(3) and Leu(4) NH groups show limited solvent accessibility. Extensive difference nuclear Overhauser effect (n.O.e.) studies establish the occurrence of several diagnostic inter-residue n.O.e.s (Ci alpha H----Ni+1H and NiH----Ni+1H) between backbone protons. The simultaneous observation of "mutually exclusive" n.O.e.s suggests the presence of multiple solution conformations for both peptides. In peptide 1 the n.O.e. data are consistent with a dynamic equilibrium between an -Ala-delta Z-Phe- Type II beta-turn structure and a second species with delta Z-Phe adopting a partially extended conformation with psi values of +/- 100 degrees to +/- 150 degrees. In peptide 2 the results are compatible with an equilibrium between a highly folded consecutive beta-turn structure for the -Leu-delta Z-Phe-Ala- segment and an almost completely extended conformation.
3. Enzymatic peptide synthesis in organic media: a comparative study of water-miscible and water-immiscible solvent systems
P Clapés, P Adlercreutz, B Mattiasson J Biotechnol. 1990 Sep;15(4):323-38. doi: 10.1016/0168-1656(90)90090-x.
Peptide synthesis was carried out in a variety of organic solvents with low contents of water. The enzyme was deposited on the support material, celite, from an aqueous buffer solution. After evaporation of the water the biocatalyst was suspended in the reaction mixtures. The chymotrypsin-catalyzed reaction between Z-Phe-OMe and Leu-NH2 was used as a model reaction. Under the conditions used ([Z-Phe-OMe]0 less than or equal to 40 mM, [Leu-NH2]0/([Z-Phe-OMe]0 = 1.5) the reaction was first order with respect to Z-Phe-OMe. Tris buffer, pH 7.8, was the best buffer to use in the preparation of the biocatalyst. In water-miscible solvents the reaction rate increased with increasing water content, but the final yield of peptide decreased due to the competing hydrolysis of Z-Phe-OMe. Among the water-miscible solvents, acetonitrile was the most suitable, giving 91% yield with 4% (by vol.) water. In water-immiscible solvents the reaction rate and the product distribution were little affected by water additions in the range between 0% and 2% (vol. %) in excess of water saturation. The reaction rates correlated well with the log P values of the solvent. The highest yield (93%) was obtained in ethyl acetate; in this solvent the reaction was also fast. Under most reaction conditions used the reaction product was stable; secondary hydrolysis of the peptide formed was normally negligible. The method presented is a combination of kinetically controlled peptide synthesis (giving high reaction rates) and thermodynamically controlled peptide synthesis (giving stable reaction products).
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