109425-49-2

Usage

Uses

Used in Pharmaceutical Synthesis:
FMOC-VAL-PRO-OH is used as a reactant in the synthesis of a double prodrug of anti-varicella zoster virus bicyclic nucleoside analogs. This application is significant because it aids in the development of novel antiviral agents that can effectively combat the varicella zoster virus, which is responsible for causing chickenpox and shingles.
In the synthesis process, FMOC-VAL-PRO-OH serves as a key intermediate, providing a protected peptide sequence that can be further modified or conjugated to other molecules to enhance the pharmacological properties of the final prodrug. The Fmoc group is particularly useful as it allows for selective deprotection and coupling reactions, facilitating the assembly of complex peptide-based structures.
Overall, FMOC-VAL-PRO-OH plays a crucial role in the advancement of antiviral drug development, offering a valuable synthetic tool for the creation of innovative therapeutic agents targeting the varicella zoster virus.

Downstream Products

• 20488-27-1 (S)-1-((S)-2-Amino-3-methyl-butyryl)-pyrrolidine-2-carboxylic acid 
• 1403230-61-4 3-[2’-deoxy-5’-O-[2-(valylprolylamino)ethylcarbamoyl]-β-D-ribofuranosyl]-6-(p-pentylphenyl)-2,3-dihydrofuro[2,3-d]pyrimidin-2-one 
• 1403230-69-2 3-[3’-O-(tert-butyldimethylsilyl)-2’-deoxy-5’-O-[2-(valylprolylamino)ethylcarbamoyl]-β-D-ribofuranosyl]-6-(p-pentylphenyl)-2,3-dihydrofuro[2,3-d]pyrimidin-2-one 
• 1269409-96-2 3-[2'-deoxy-5'-O-[N-(fluorenylmethoxycarbonyl)valylprolylphenylalanyl]-β-D-ribofuranosyl]-6-(p-pentylphenyl)-2,3-dihydrofuro[2,3-d]pyrimidin-2-one 
• 1269409-94-0 3-[2'-deoxy-5'-O-[N-(fluorenylmethoxycarbonyl)valylprolylleucyl]-β-D-ribofuranosyl]-6-(p-pentylphenyl)-2,3-dihydrofuro[2,3-d]pyrimidin-2-one 
• 1127417-04-2 3-[5'-O-(tert-butyldimethylsilyl)-2'-deoxy-3'-O-[N-(fluorenylmethoxycarbonyl)valylprolylvalyl]-β-D-ribofuranosyl]-6-(p-pentylphenyl)-2,3-dihydrofuro[2,3-d]pyrimidin-2-one 
• 1127417-11-1 3-[2'-deoxy-3',5'-bis-O-[N-(fluorenylmethoxycarbonyl)valylprolylvalyl]-β-D-ribofuranosyl]-6-(p-pentylphenyl)-2,3-dihydrofuro[2,3-d]pyrimidin-2-one 
• 1269409-99-5 3-[2'-deoxy-5'-O-(valylprolylalanyl)-β-D-ribofuranosyl]-6-(p-pentylphenyl)-2,3-dihydrofuro[2,3-d]pyrimidin-2-one 
• 1269409-98-4 3-[2'-deoxy-5'-O-[N-(fluorenylmethoxycarbonyl)valylprolylalanyl]-β-D-ribofuranosyl]-6-(p-pentylphenyl)-2,3-dihydrofuro[2,3-d]pyrimidin-2-one 
• 1127416-93-6 3-[2'-deoxy-5'-O-[N-(fluorenylmethoxycarbonyl)valylprolylvalyl]-β-D-ribofuranosyl]-6-(p-pentylphenyl)-2,3-dihydrofuro[2,3-d]pyrimidin-2-one 

Relevant academic research and scientific papers

Functional identification and structure determination of two novel prolidases from cog1228 in the amidohydrolase superfamily

Two uncharacterized enzymes from the amidohydrolase superfamily belonging to cog1228 were cloned, expressed, and purified to homogeneity. The two proteins, Sgx9260c (gi|44242006) and Sgx9260b (gi|44479596), were derived from environmental DNA samples originating from the Sargasso Sea. The catalytic function and substrate profiles for Sgx9260c and Sgx9260b were determined using a comprehensive library of dipeptides and N-acyl derivative of l-amino acids. Sgx9260c catalyzes the hydrolysis of Gly-l-Pro, l-Ala-l-Pro, and N-acyl derivatives of l-Pro. The best substrate identified to date is N-acetyl-l-Pro with a value of kcat/Km of 3 × 105 M -1 s-1. Sgx9260b catalyzes the hydrolysis of l-hydrophobic l-Pro dipeptides and N-acyl derivatives of l-Pro. The best substrate identified to date is N-propionyl-l-Pro with a value of kcat/Km of 1 × 105 M-1 s-1. Three-dimensional structures of both proteins were determined by X-ray diffraction methods (PDB codes 3MKV and 3FEQ). These proteins fold as distorted (β/α) 8-barrels with two divalent cations in the active site. The structure of Sgx9260c was also determined as a complex with the N-methylphosphonate derivative of l-Pro (PDB code 3N2C). In this structure the phosphonate moiety bridges the binuclear metal center, and one oxygen atom interacts with His-140. The α-carboxylate of the inhibitor interacts with Tyr-231. The proline side chain occupies a small substrate binding cavity formed by residues contributed from the loop that follows β-strand 7 within the (β/α)8-barrel. A total of 38 other proteins from cog1228 are predicted to have the same substrate profile based on conservation of the substrate binding residues. The structure of an evolutionarily related protein, Cc2672 from Caulobacter crecentus, was determined as a complex with the N-methylphosphonate derivative of l-arginine (PDB code 3MTW).