Z-Gly-OH

Z-Gly-OH

Peptide ionophores: synthesis and cation-binding properties of a bicyclic peptide containing glycine and lysine residues.[Pubmed:7655187]

Pept Res. 1995 Mar-Apr;8(2):62-9.

Peptide 1, cyclo(1,5-epsilon-succinoyl) (Lys-Gly-Gly-Gly)2, is a representative member of a family of polycyclic peptide ionophores characterized by C2 symmetry and a relatively flexible structure resulting from its high Gly content. Peptide 1 has been synthesized by two different solid-phase protocols from its linear precursors, H-Gly-Gly-Lys(Fmoc)-Gly-Gly-Gly-Lys(Fmoc)-Gly-OH and H-Gly-Gly-Lys(Z)-Gly-Gly-Gly-Lys(Z)-Gly-OH), and satisfactorily characterized by chemical means. The CD spectrum of 1 is compatible with a beta-folded structure, stabilized by two internal hydrogen bonds. The complexation behavior of 1 toward alkaline and alkaline-earth cations can be envisaged as an equilibrium between inclusion (1:1) and sandwich (2:1) complex models, with affinities in the 10(6) M-1 and 10(11) M-2 range, respectively. A slight preference of 1 for Sr2+ over other cations has been found.

Ligand bindings of bovine carboxypeptidase B. III. Hydrophobic activators in dipeptide hydrolysis.[Pubmed:7400116]

J Biochem. 1980 Jun;87(6):1681-9.

Several hydrophobic compounds acted as activators in dipeptide (Bz-Gly-L-Arg-OH, Z-Gly-L-Phe-OH) hydrolysis by bovine carboxypeptidase B. These hydrophobic compounds include BZ-Gly-OH, Z-Gly-OH, Z-L-Phe-OH, and Z-L-Phe-GLy-OH. These compounds were indicated to bind to the secondary substrate binding sites which is proposed to be responsible for substrate activation kinetics in dipeptide hydrolysis. Of the compounds Z-L-Phe-OH alone acted also as a inhibitor at higher concentrations, indicating that it binds to both primary and secondary sites as the dipeptide substrates do. Comparison of the activation effects of the compounds employed indicated that hydrophobic interaction played an important role in binding to the secondary site. Substrate and modifier binding constants were also determined and the results indicated that modifier binding increased both affinity and catalytic rate constant of the primary site. On the other hand, Z-Gly-OH and Z-L-Phe-Gly-OH inhibited the hydrolyses of tri and tetrapeptide substrates. This observation suggests that the secondary site is contained in the extended active center which the enzyme possibly has.

The 1,3-dipolar cycloaddition reaction in the functionalization of carbon nanofibers.[Pubmed:18330154]

J Nanosci Nanotechnol. 2007 Oct;7(10):3441-5.

Carbon nanofibers were functionalized using a reaction scheme described in the literature for 1,3-dipolar cycloaddition of azomethine ylides generated in situ by the condensation of an alpha-amino acid and an aldehyde. The reagents used were Z-Gly-OH and paraformaldehyde. Their reaction with carbon nanofibers was studied as a solid mixture by controlled heating in the DSC. An oxazolidinone intermediate was formed as the major product. Z-Gly-OH and paraformaldehyde were also reacted with a model compound (anthracene) in DMF solution leading to the formation of a considerable amount of anthraquinone. These studies suggested that, under the conditions investigated, the 1,3-dipolar cycloaddition reaction was not favoured, and the main result of functionalization was the formation of quinone-type groups as a consequence of an oxidation process.