51871-42-2

Usage

Uses

Used in Biochemical Research:
BOC-GLY-LEU-OH is used as a peptide building block for the synthesis of various biochemical compounds. Its protective t-BOC group ensures that undesired reactions are prevented during the synthesis process, allowing for the creation of complex molecular structures.
Used in Pharmaceutical Industry:
BOC-GLY-LEU-OH is used as a raw material for the development of pharmaceutical compounds. Its unique structure, including the protective t-BOC group and the combination of glycine and leucine amino acids, makes it a valuable component in the creation of new drugs and therapeutic agents.
Used in Cosmetics Industry:
BOC-GLY-LEU-OH is used as an active ingredient in cosmetic products for its potential benefits to the skin. The combination of amino acids and the hydroxyl group may contribute to improved skin hydration, elasticity, and overall health.
Used in Food Industry:
BOC-GLY-LEU-OH is used as a functional ingredient in the food industry, where its unique properties may contribute to improved taste, texture, or nutritional value of food products. The presence of amino acids and the hydroxyl group can enhance the sensory experience and provide potential health benefits.
Used in Agricultural Industry:
BOC-GLY-LEU-OH is used as a component in the development of biopesticides or plant growth regulators. Its unique structure may contribute to the enhancement of plant resistance against pests or diseases, promoting healthier and more sustainable agricultural practices.

Upstream product

• 4530-20-5 BOC-glycine 
• 3392-07-2 tert-butyl N-{2-[(2,5-dioxopyrrolidin-1-yl)oxy]-2-oxoethyl}carbamate 
• 61-90-5 L-leucine 
• 869-19-2 Glycyl-L-leucine 
• 24424-99-5 di-tert-butyl dicarbonate 
• 67084-40-6 1-(N-tert-butoxycarbonyl-glycyloxy)-1H-benzotriazole 
• 2666-93-5 (S)-Leu-OMe 
• 17790-86-2 tert-butyl 2-oxo-2-(2-phenylhydrazinyl)ethylcarbamate 
• 77162-21-1 Boc-Gly-Leu-NHNHPh 
• 202265-96-1 N-tert-butyloxycarbonyl-L-glycyl-L-leucine 2-methoxyethyl ester 
• 7535-69-5 (S)-methyl 2-(2-((tert-butoxycarbonyl)amino)acetamido)-4-methylpentanoate 

Downstream Products

• 76487-61-1 Z-Aib-Pro-Aib-Ala-Aib-Ala-Gln-Aib-Val-Aib-Gly-Leu-Aib-OH 
• 76487-60-0 Z-Aib-Pro-Aib-Ala-Aib-Ala-Gln-Aib-Val-Aib-Gly-Leu-Aib-OMe 
• 1340584-80-6 Boc-Gly-L-Leu-L-Cys(S-Cbz-L-Ala)-Gly-OCH₃ 
• 1340584-81-7 H-Gly-L-Leu-L-Cys(S-Cbz-L-Ala)-Gly-OCH₃ hydrochloride 
• 1340584-83-9 C₃₆H₄₈N₆O₁₁S 
• 1340585-01-4 C₅₀H₇₂N₁₀O₁₆S₂ 
• 108456-25-3 methyl (2S,5S)-2-benzyl-8-[(tert-butoxycarbonyl)amino]-5-isobutyl-4,7-dioxo-3,6-diazaoctanoate 
• 118700-52-0 Boc-Gly-Leu-Gly-OBzl 
• 474317-02-7 Boc-Gly-Leu-Met-Gly-Met-Gly-NHNHPh 

Relevant academic research and scientific papers

Stereoretentive Reactions at the Anomeric Position: Synthesis of Selenoglycosides

Reported is the stereospecific cross-coupling of anomeric stannanes with symmetrical diselenides, resulting in the synthesis of selenoglycosides with exclusive anomeric control. The reaction proceeds without the need for directing groups and is compatible

Microwave-Assisted Synthesis of 2,2′-Azopyridine-Labeled Amines, Amino Acids, and Peptides

A microwave-assisted procedure for labeling amines, amino acids, and peptides with 2,2′-azopyridines (2,2′-AzPy) is described using the corresponding 2,2′-azopyridine-diacylbenzotriazoles. The efficiency of the procedure is proven by the generation of thr

Microwave-assisted chemical ligation of S-acyl peptides containing non-terminal cysteine residues

An efficient approach for the synthesis of a series of S-acyl peptides containing internal cysteine residues has been developed and the chemical long-range ligation of these S-acyl peptides via 5-, 8-, 11- and 14-membered cyclic transition states has been

Synthesis and pharmacological investigation of segetalin C as a novel antifungal and cytotoxic agent

In present study, a natural phenylalanine-rich cycloheptapeptide segetalin C (compound VIII) was synthesized by coupling and cyclization of peptide units Boc-gly-L-leu-L-his-OH and L-Phe-L-ala-L-phe-L-pro-OMe and examined for different bioactivities. The

Phenylhydrazide as an enzyme-labile protecting group in peptide synthesis

The enzymatic cleavage of amino acid phenylhydrazides with the enzyme tyrosinase (EC 1.14.18.1) offers a new, mild, and selective method for C-terminal deprotection of peptides. The advantages of the described methodology are the very mild oxidative removal of the protecting group at room temperature and pH 7, a high chemo- and regioselectivity, and the availability of the biocatalyst. Even in oxygen-saturated solution, the oxidation of sensitive methionine residues was not observed. These features make the methodology suitable for the synthesis of sensitive peptide conjugates. Mechanistic data suggest that the hydrolysis of the oxidized adducts proceeds by a free-radical mechanism.

Comparative lipase-catalyzed hydrolysis of ethylene glycol derived esters. The 2-methoxyethyl ester as a protective group in peptide and glycopeptide synthesis

Comparison of the lipase-catalyzed cleavage of polar esters derived from ethylene glycol proved 2-methoxyethyl (ME) esters most favorable protecting groups for the carboxylic function of peptides and glycopeptides. They combine high substrate acceptance and iligh yields of hydrolysis with favorable physicochemical properties and advantageous solubility. The application of this polar ester as protecting group was extended to N-glycosylated amino acids and N-glycopeptides. The selective removal of ME esters by lipases was achieved under mild conditions (pH 7.0 and 37°C), leaving all other linkages including peptide bonds and other ester protecting groups unaffected.

Polypeptide derivatives

Novel synthetic polypeptide derivatives, i.e., novel calcitonin derivatives, having improved basic physiological activities of the corresponding natural calcitonins, i.e., the activity for lowering the blood level of calcium, the activity as an analgesic, as well as the activity for inhibiting the secretion of the gastric juice. Thus these synthetic calcitonins are effective as agents for curing hypercalcemia, analgetic agents, anti-ulcerative agents and the like.

SOLUTION PHASE SYNTHESIS OF ALAMETHICIN I

The total synthesis of alamethicin I by solution phase methods is reported.

Synthetic antigens of luteinizing hormone releasing hormone

Synthetic antigens related to luteinizing hormone-releasing hormone (hereinafter designated LH-RH) having the amino acid composition, pyroglutamyl-histidyl-tryptophanylseryl-tyrosyl-glycyl-leucyl-arginyl-prolyl-glycyl-poly-L-lysine (hereinafter designated pyroglu-his-trp-ser-tyr-glyleu-arg-pro-gly-poly-L-lys) and poly-L-lysyl-glutarylhistidyl-tryptophanyl-seryl-tyrosyl-glycyl-leucyl-arginylprolyl-glycine amide (hereinafter designated poly-L-lysglutaryl-his-trp-ser-tyr-gly-leu-arg-pro-gly) are prepared by coupling the corresponding decapeptide with poly-L-lysine. The corresponding decapeptides are prepared by controlled stepwise procedures starting with individual amino acid components. These antigens have the property of inducing formation of antibodies to luteinizing hormone-releasing hormone (LH-RH) in animals.