138372-76-6

Usage

Uses

Used in Peptide Synthesis:
L-Proline, 1-[N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-phenylalanyl]is used as a building block in peptide synthesis for the creation of complex peptide sequences. The Fmoc protecting group allows for the stepwise addition of amino acids, facilitating the synthesis of peptides with specific sequences and functions.
Used in Solid-Phase Peptide Synthesis (SPPS):
In the pharmaceutical and biotechnology industries, L-Proline, 1-[N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-phenylalanyl]is utilized as a key component in solid-phase peptide synthesis. This technique involves the stepwise assembly of peptides on an insoluble resin support, with the Fmoc group playing a critical role in protecting the amino acid's side chain during the synthesis process.
Used in Research Applications:
L-Proline, 1-[N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-phenylalanyl]is employed as a research tool for studying the structure, function, and interactions of peptides and proteins. Its controlled synthesis capabilities allow scientists to investigate the properties of specific peptide sequences and their potential applications in various biological systems.
Used in Therapeutic Applications:
In the development of peptide-based drugs, L-Proline, 1-[N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-phenylalanyl]is used to synthesize bioactive peptides with potential therapeutic effects. The precise control over peptide synthesis provided by the Fmoc group enables the production of peptides with specific pharmacological properties, such as improved stability, bioavailability, and target specificity.

Upstream product

• 35661-40-6 N-Fmoc L-Phe 
• 101214-43-1 Fmoc-Phe-ONSu 
• 147-85-3 L-proline 

Downstream Products

• 7669-65-0 L-phenylalanyl-L-proline 
• 663949-73-3 Fmoc-Phe-Pro-NHMe 

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).

Factors Affecting Conformation in Proline-Containing Peptides

(Equation presented) NMR was used to study the thermodynamics of the cis → trans isomerization for prolyl amide bonds in the compounds shown. The magnitude of Kt/c for C-terminal esters is greater than for the corresponding amides, signifying s