77167-53-4

Usage

Uses

Used in Pharmaceutical and Research Applications:
L-Leucine, L-leucyl-, phenylmethyl ester is utilized as a building block in the synthesis of peptides and proteins, contributing to the development of novel therapeutic agents and research tools. Its role in these applications is to facilitate the assembly of complex peptide structures, which can be further explored for their potential biological activities and medicinal properties.
Used in Peptide Synthesis:
In the field of peptide synthesis, L-Leucine, L-leucyl-, phenylmethyl ester is employed as a protected amino acid derivative. The phenylmethyl ester group protects the carboxylic acid functionality, allowing for selective reactions and preventing unwanted side reactions during the synthesis process. This protection is crucial for the successful construction of larger peptide chains with specific sequences and desired properties.
It is important to handle L-Leucine, L-leucyl-, phenylmethyl ester with care and in accordance with proper safety guidelines due to its potential for toxicity and irritancy, ensuring the safety of researchers and the integrity of the experimental procedures.

Upstream product

• 1738-77-8 L-leucine benzyl ester p-toluenesulfonate 
• 3190-70-3 L-leucine N-carboxyanhydride 
• 1738-69-8 L-Leucine benzyl ester 
• 1013661-54-5 C₃₄H₄₀N₂O₅ 
• 35661-60-0 Fmoc-Leu-OH 
• 100-39-0 benzyl bromide 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 32925-57-8 Boc-Leu-Leu-OBzl 
• 66450-17-7 Boc-Leu-HONB 
• 87746-56-3 2-tert-butoxycarbonylamino-4-methyl-penatnoic acid benzyl ester 

Downstream Products

• 3303-31-9 L-leucyl-L-leucine 

Relevant academic research and scientific papers

Glycopeptide probes for understanding peptide specificity of the folding sensor enzyme UGGT

A systematic series of chitobiose-modified pentapeptides with sequence variations of hydrophobic leucine and hydrophilic serine were synthesized. The resulting glycopeptides were used as molecular probes to elucidate aglycon peptide specificity of the gly

From peptides to their alternating ester-urea analogues: Synthesis and influence of hydrogen bonding motif and stereochemistry on aggregation

(Chemical Equation Presented) Peptide-mimicking scaffolds with an incorporated ester-urea motif, replacing two adjacent amide residues, were synthesized and their aggregation behavior was studied in dependence of hydrogen bonding sites as well as backbone stereochemistry. Two oligomer series containing either 50% or 100% ester-urea units and either all-(L) or (D)-alt-(L) backbone configuration were prepared via ester and amide couplings, using a divergent/convergent exponential growth strategy. Their aggregation behavior in organic solution was investigated by means of concentration-dependent NMR spectroscopy and compared to the parent peptide series. Interestingly, the naturally occurring peptide scaffold exhibits the largest tendency to associate in combination with the strongest difference in aggregation behavior between all-(L) and (D)-alt-(L) backbone stereochemistry. With increasing incorporation of the ester-urea motif the aggregation strength decreases and become much less dependent on the backbone configuration. The obtained structure-aggregation relationships reveal the importance of the commensurability and multivalency of hydrogen bonding sites as well as conformational restriction for peptide association and should hence aid the design of peptide mimics, such as β -sheet breakers or gelators. 2009 American Chemical Society.

Application of a unique automated synthesis system for solution-phase peptide synthesis

An automated synthesis system, which is suitable for repetitive syntheses using similar reaction procedures, was used to synthesize systematically a library of all possible dipeptides (25) and tripeptides (125) from 5 protected amino acids. The apparatus has also been applied to the automated synthesis of 10 fragment tripeptide derivatives that are constituents of the hormone PACAP-27. The measured molecular optical rotation values of the library of 125 tripeptides were found to correlate well with calculated values obtained by summation of the molecular optical rotation values for the constituent amino acids.

The Steric Hindrance of the Stepwise Reaction of N-Carboxy α-Amino Acid Anhydride with the α-Amino Acid Ester

The mechanisms of the reactions of 4-alkyloxazolidinediones (1) (N-carboxy α-amino acid anhydrides(NCAs)) with α-amino acid benzyl ester p-toluenesulfonates (2) were investigated in acetonitrile containing triethylamine at low and room temperatures.Two types of reactions were observed: (1) the polymerization of NCAs was initiated with a small amount of 2 to produce polypeptides (6), and (2) the dipeptide benzyl esters (4) were produced by the stepwise reaction of NCAs with the esters.Both the polymerization and the dipeptide formation (1+2) seemed to be initiated by the nucleophilic attack of the amino group of the ester on the C-5 carbon of NCAs.The polymerization proceeded when the side chains of the amino acid esters (R2) were more bulky than those of the NCAs (R1).On the contrary, dipeptide esters were produced when the side chains of the NCAs (R1) were more bulky than those of the esters (R2).