247217-28-3

Usage

Uses

Used in Pharmaceutical Industry:
Pentanedioic acid, 3-[[(9H-fluoren-9-ylmethoxy)carbonyl]amino]is used as a building block for the synthesis of peptides and peptide-based drugs. Its Fmoc protecting group allows for the stepwise addition of amino acids during peptide synthesis, enabling the production of complex peptide sequences.
Used in Biotechnology Industry:
Pentanedioic acid, 3-[[(9H-fluoren-9-ylmethoxy)carbonyl]amino]is used as a component in the development of biotechnological applications, such as the production of recombinant proteins and the design of peptide-based therapeutics. Its versatility in peptide synthesis allows for the creation of novel bioactive molecules with potential applications in various fields.

Upstream product

• 1246651-90-0 Fmoc-β-Glu(OBu-t)-OH 
• 247217-26-1 3-(N-tert-butyloxycarbonylamino)-4-cyano benzylbutyrate 
• 247217-27-2 3-(N-fluorenylmethoxycarbonylamino)-4-cyano benzylbutyrate 

Downstream Products

• 247217-33-0 (S)-2-[3-(9H-Fluoren-9-ylmethoxycarbonylamino)-4-((S)-1-methoxycarbonyl-2-phenyl-ethylcarbamoyl)-butyrylamino]-3-phenyl-propionic acid methyl ester 

Relevant academic research and scientific papers

18F-FP-PEG2-β-Glu-RGD2: A symmetric integrin αvβ3-targeting radiotracer for tumor PET imaging

Radiolabeled cyclic arginine-glycine-aspartic (RGD) peptides can be used for noninvasive determination of integrin αvβ3 expression in tumors. In this study, we performed radiosynthesis and biological evaluation of a new 18

Synthesis and conformation of dipeptide taste ligands containing homo-β-amino acid residues

The synthesis and conformational properties of a series of dipeptide taste ligands, differing from the commercial sweetener aspartame by the presence of a methylene group between the Cα and the C′ carbon atoms (as in homo-β-residues) in either the L-Asp or the L-Phe residues, are described. Homo-β-residues such as homo-β-aspartic acid, homo-β-phenylglycine and homo-β-phenylalanine, obtained by homologation of the corresponding proteinogenic α-amino acids, have been used in the solution peptide synthesis of the following aspartame analogues in protected and unprotected forms: NH2-homo-β-(L or D)-Asp-L-Phe-OMe, NH2-L-Asp-homo-β-L-Phg-OMe and NH2-L-Asp-homo-β-L-Phe-OMe. Lengthening of the peptide skeleton at the L-Asp site results in a drastic loss of sweetness with the production of tasteless compounds; on the other hand, lengthening of the skeleton at the C-terminal L-Phe site partially mantains the sweet taste in both NH2-L-Asp-hamo-β-L-Phe-OMe and NH2-L-Asp-homo-β-L-Phg-OMe. The solution conformation of the synthesized dipeptide taste ligands was investigated by NMR and circular dichroism techniques. The analysis of NMR data combined with restrained molecular dynamics calculations shows that all peptides are fairly flexible and they do not assume a preferred conformation in DMSO and methanol. The peptides containing homo-β-L-Phe and homo-β-L-Phg do adopt a discrete number of conformation among which mainly extended and 'L-shaped' conformation are represented The circular dichroism spectra are consistent with the NMR results, indicating a significant flexibility for these compounds. Copyright