4467-55-4

Usage

Uses

Used in Drug Development:
Z-D-VAL-OSU is used as a research tool for drug development, enabling the study of protein targets and the development of novel therapeutic agents that can modulate protein function for treating various diseases.
Used in Structural Biology:
In the field of structural biology, Z-D-VAL-OSU is used as a protein-modifying agent to facilitate the determination of protein structures and the understanding of protein dynamics, which is crucial for elucidating the mechanisms of biological processes and designing effective drugs.
Used in Biochemical Pathway Exploration:
Z-D-VAL-OSU is employed as a research compound in the exploration of biochemical pathways, allowing scientists to investigate the roles of specific proteins in cellular processes and identify potential targets for therapeutic intervention.
Used in Protein-Protein Interaction Studies:
Z-D-VAL-OSU is utilized as a tool for studying protein-protein interactions, providing insights into the molecular mechanisms underlying various biological functions and the development of new strategies for modulating these interactions in disease treatment and prevention.

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 1685-33-2 N-[(benzyloxy)carbonyl]-D-valine 

Downstream Products

• 17572-36-0 Carbobenzoxy-D-Val-D-Phe 
• 22221-75-6 Z-D-Val-Gly-OH 
• 138754-84-4 (R)-3-methyl-1-oxobutane-2-benzylcarbamate 
• 260978-43-6 benzyl (1R)-1-(hydroxymethyl)-2-methylpropylcarbamate 
• 1092975-16-0 C₂₈H₃₈N₄O₆ 
• 1092975-14-8 C₃₂H₄₄N₄O₆ 
• 146766-11-2 (R)-2-((R)-2-Benzyloxycarbonylamino-3-methyl-butyrylamino)-3-phenyl-propionic acid 2,5-dioxo-pyrrolidin-1-yl ester 
• 146766-13-4 {(R)-1-[(R)-1-(2-Chloro-ethylcarbamoyl)-2-phenyl-ethylcarbamoyl]-2-methyl-propyl}-carbamic acid benzyl ester 

Relevant academic research and scientific papers

Efficient access to enantiopure γ4-amino acids with proteinogenic side-chains and structural investigation of γ4- asn and γ4-ser in hybrid peptide helices

Hybrid peptides composed of α- and β-amino acids have recently emerged as new class of peptide foldamers. Comparatively, γ- and hybrid γ-peptides composed of γ4-amino acids are less studied than their β-counterparts. However, recent investigations reveal that γ4-amino acids have a higher propensity to fold into ordered helical structures. As amino acid side-chain functional groups play a crucial role in the biological context, the objective of this study was to investigate efficient synthesis of γ4-residues with functional proteinogenic side-chains and their structural analysis in hybrid-peptide sequences. Here, the efficient and enantiopure synthesis of various N- and C-terminal free-γ4-residues, starting from the benzyl esters (COOBzl) of N-Cbz-protected (E)-α,β-unsaturated γ-amino acids through multiple hydrogenolysis and double-bond reduction in a single-pot catalytic hydrogenation is reported. The crystal conformations of eight unprotected γ4-amino acids (γ4-Val, γ4-Leu, γ4-Ile, γ4-Thr(OtBu), γ4-Tyr, γ4-Asp(OtBu), γ4- Glu(OtBu), and γ-Aib) reveals that these amino acids adopted a helix favoring gauche conformations along the central Cγi￡ Cβ bond. To study the behavior of γ4- residues with functional side chains in peptide sequences, two short hybrid γ-peptides P1 (Ac-Aib-γ4-Asn-Aib-γ4-Leu- Aib-γ4-Leu-CONH2) and P2 (Ac-Aib- γ4-Ser-Aib-γ4-Val-Aib-γ4-Val- CONH2) were designed, synthesized on solid phase, and their 12-helical conformation in single crystals were studied. Remarkably, the γ4-Asn residue in P1 facilitates the tetrameric helical aggregations through interhelical H bonding between the side-chain amide groups. Furthermore, the hydroxyl side-chain of γ4-Ser in P2 is involved in the interhelical H bonding with the backbone amide group. In addition, the analysis of 87 γ4-residues in peptide single-crystals reveal that the γ4-residues in 12-helices are more ordered as compared with the 10/12- and 12/14-helices. Copyright

New chiral tetraaza ligands for the efficient enantioselective addition of dialkylzinc to aromatic aldehydes

A series of chiral tetraaza ligands were studied for the enantioselective addition of dialkylzinc to aldehydes. These bis(amino amide) ligands show high enantioselectivity in the addition of organozincs to aromatic aldehydes. Different structural elements on the ligands seem to play an important role in determining the observed enantioselectivity. Ligand 4b (N,N′-bis(N-l-valinyl)-1,3-diaminopropane, with an aliphatic spacer with 3C atoms) catalyzed the addition of Et2Zn to benzaldehyde, 1-naphtaldehyde, 4-methoxybenzaldehyde, and 4-chlorobenzaldehyde to give the corresponding alcohol products with excellent conversions and selectivities and with enantioselectivities of 99, 97, 98, and 82%, respectively. DFT calculations provide an understanding of the mechanism of the enantioselection process.

In the search for new anticancer drugs. XXIV: Synthesis and anticancer activity of amino acids and dipeptides containing the 2-chloroethyl- and [N'- (2-chloroethyl)-N'-nitroso]-aminocarbonyl groups

A series of L,L-(42, 44, 46, and 60) and D,D-(43, 45, 47, and 61) dipeptide derivatives composed of phenylglycine, phenylalanine, homophenylalanine, and valine and containing a 2-chloroethylamino group at the C-terminus and an N'-(2-chloroethyl)-N'-nitrosoaminocarbonyl group at the N-terminus of the dipeptides were prepared. The dipeptide derivatives (42- 47, 60, and 61) were first evaluated in vivo for their anticancer activities against the murine lymphocytic leukemia P388. Compounds 42, 44, 46, and 60 possessed activities ranging from 46 to 111 percent increase in life span (%ILS), whereas 43 was marginal (%ILS = 31) and 45, 47, and 61 were inactive. In general, the L,L-series exhibited low to good activity (%ILS = 46-111), whereas the corresponding D,D-series, except for 43 (%ILS = 31), was devoid of activity. The analogously structured monoamino acid derivatives of L- alanine (74), L-phenylalanine (75), and L-aspartic acid (76) exhibited higher activity against P388 than the dipeptide derivatives (i.e., 481, 297, and 481 %ILS, respectively). The more active representatives of dipeptides (i.e., 42, 44, and 60) and the amino acids derivatives 74-76 were then tested in vivo against the murine lymphoid leukemia L1210. Compounds 42, 44, and 60 exhibited either low or marginal activity (i.e., the %ILS values were 46, 31, and 26, respectively). Compounds 74, 75, and 76 possessed low to moderate activity, as evidenced by the %ILS values of 56, 48, and 64, respectively. The %ILS parameters obtained against the P388 and L1210 tumor lines were correlated with the corresponding lipophilicities, and there is a trend towards higher activity with concomitant decrease in hydrophobicity.