38136-75-3

Usage

Uses

Used in Peptide and Protein Research:
H-TRP-PRO-OH is used as a building block for the synthesis of peptides and proteins, facilitating the study and development of novel bioactive molecules.
Used in Pharmaceutical Development:
H-TRP-PRO-OH is utilized as a component in the creation of new pharmaceuticals, leveraging its ability to mimic natural peptides for therapeutic purposes.
Used in Biotechnology Products:
H-TRP-PRO-OH is employed in the development of biotechnology products, contributing to the advancement of innovative solutions in various industries.
Used in Drug Delivery:
H-TRP-PRO-OH is used as a component in drug delivery systems, potentially enhancing the efficacy and targeting of therapeutic agents.
Used in Immunotherapy:
H-TRP-PRO-OH is applied in immunotherapy, where it may contribute to the development of treatments that modulate immune responses.
Used as a Research Tool for Protein-Protein Interactions:
H-TRP-PRO-OH serves as a tool for studying protein-protein interactions, providing insights into the mechanisms of various biological processes.
Used in Studying Structure-Function Relationships:
H-TRP-PRO-OH is used to investigate structure-function relationships in proteins, aiding in the understanding of their roles in biological systems.

Upstream product

• 126689-19-8 4-(3-indolylmethyl)-2-trifluoromethyl-5(4H)-oxazolone 
• 153-94-6 D-tryptophan 
• 120151-94-2 1,7-dioxo-2,5,6-trimethyl-1H,7H-pyrazolo<1,2-a>pyrazol-3-yl-methylthiomethylcarbonyl-glycyl-L-tryptophyl-L-proline 
• 120151-96-4 1,7-dioxo-2,5,6-trimethyl-1H,7H-pyrazolo<1,2-a>pyrazol-3-yl-methylthiomethylcarbonyl-L-phenylalanyl-l-tryptophyl-L-proline 
• 251316-94-6 C₃₁H₂₉N₃O₅ 

Downstream Products

• 67889-75-2 brevianamide F 
• 120151-96-4 1,7-dioxo-2,5,6-trimethyl-1H,7H-pyrazolo<1,2-a>pyrazol-3-yl-methylthiomethylcarbonyl-L-phenylalanyl-l-tryptophyl-L-proline 

Relevant academic research and scientific papers

REACTION OF TRYPTOPHAN WITH TRIFLUOROACETIC ANHYDRIDE

Trifluoroacetic anhydride (TFAA) in ether quickly (=5-10 min) converted tryptophan to the crystalline 2-trifluoromethyl-5(4H)-oxazolone (2) without racemization.Dissolution of optically active 2 in acetonitrile gave racemic 2, whereas treatment with hot aqueous dioxane gave the isomeric oxazolone (3).Both 2 and 3, could on heating be further isomerized to the conjugated oxazolone (4).These oxazolones are interesting starting materials for the preparation of tryptophan containing peptides.

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).