4249-25-6

Usage

Uses

Used in Pharmaceutical Industry:
H-GLY-LEU-OME HCL is used as a building block for the synthesis of peptides and proteins, which are essential for various biological functions and therapeutic applications. The presence of glycine and leucine, essential amino acids, makes it a valuable component in the development of new drugs and therapies.
Used in Peptide Research:
H-GLY-LEU-OME HCL is used as a research tool for studying the structure, function, and interactions of peptides. Its unique composition allows researchers to investigate the properties of specific amino acid sequences and their potential applications in medicine and biotechnology.
Used in Drug Delivery Systems:
H-GLY-LEU-OME HCL can be used as a component in the development of drug delivery systems, where its stability and modification capabilities can enhance the effectiveness and targeted delivery of therapeutic agents.
Used in Cosmetics Industry:
H-GLY-LEU-OME HCL can be utilized in the formulation of cosmetic products, where its amino acid composition may contribute to skin health and rejuvenation by promoting collagen synthesis and providing essential nutrients for skin cells.
Used in Nutritional Supplements:
H-GLY-LEU-OME HCL can be incorporated into nutritional supplements to provide essential amino acids for protein synthesis and support overall health and well-being. Its presence in supplements may aid in muscle growth, recovery, and maintenance.

Upstream product

• 7535-69-5 (S)-methyl 2-(2-((tert-butoxycarbonyl)amino)acetamido)-4-methylpentanoate 
• 7517-19-3 methyl (L)-leucinate hydrochloride 
• 27462-45-9 2?(1,3?dioxoisoindolin?2?yl)acetyl methyl leucinate 
• 61-90-5 L-leucine 
• 17331-93-0 N-benzyloxycarbonylglycyl-L-leucine methyl ester 
• 188783-05-3 N-[N-(2-benzoyl-2-ethoxycarbonylvinyl-1)glycyl]-L-leucine methyl ester 

Downstream Products

• 58111-85-6 Z-Ser-Tyr-Gly-Leu-OMe 

Relevant academic research and scientific papers

Development of peptidomimetic hydroxamates as PfA-M1 and PfA-M17 dual inhibitors: Biological evaluation and structural characterization by cocrystallization

Plasmodium parasites causing malaria have developed resistance to most of the antimalarials in use, including the artemisinin-based combinations, which are the last line of defense against malaria. This necessitates the discovery of new targets and the development of novel antimalarials. Plasmodium falciparum alanyl aminopeptidase (PfA-M1) and leucyl aminopeptidase (PfA-M17) belong to the M1 and M17 family of metalloproteases respectively and play critical roles in the asexual erythrocytic stage of development. These enzymes have been suggested as potential antimalarial drug targets. Herein we describe the development of peptidomimetic hydroxamates as PfA-M1 and PfA-M17 dual inhibitors. Most of the compounds described in this study display inhibition at sub-micromolar range against the recombinant PfA-M1 and PfA-M17. More importantly, compound 26 not only exhibits potent malarial aminopeptidases inhibitory activities (PfA-M1 Ki = 0.11 ± 0.0002 μmol/L, PfA-M17 Ki = 0.05 ± 0.005 μmol/L), but also possesses remarkable selectivity over the mammalian counterpart (pAPN Ki = 17.24 ± 0.08 μmol/L), which endows 26 with strong inhibition of the malarial parasite growth and negligible cytotoxicity on human cell lines. Crystal structures of PfA-M1 at atomic resolution in complex with four different compounds including compound 26 establish the structural basis for their inhibitory activities. Notably, the terminal ureidobenzyl group of 26 explores the S2′ region where differences between the malarial and mammalian enzymes are apparent, which rationalizes the selectivity of 26. Together, our data provide important insights for the rational and structure-based design of selective and dual inhibitors of malarial aminopeptidases that will likely lead to novel chemotherapeutics for the treatment of malaria.

Novel thiazolidinedione-5-acetic-acid-peptide hybrid derivatives as potent antidiabetic and cardioprotective agents

Thiazolidinediones (TZDs) are one of the important clinically established antidiabetic agents. Amino-acid and peptides have an advantage of better target selectivity and specificity. As hybrids, they also improved absorption and showed better bioavailability, which in turn makes them safer. Hence, here an effort has been made to synthesize hybrids of thiazolidinedione with amino-acids and peptides and evaluate their antidiabetic and cardioprotective effect in streptozotocin-nicotinamide (STZ-NA) induced Type 2 diabetes mellitus (T2DM) rat models. A series of 14 thiazolidinedione-5-acetic acid hybrids with of different amino-acids and peptide combinations were synthesized, characterized and further screened for antidiabetic and cardioprotective activity. Among all, six compounds T1 (SSDMA1), T4 (SSDMA4), T5 (SSDMA5), T7 (SDMA13), T9 (SSDMA15) and T13 (SSDMA49) showed better antioxidant activity and comparable % glucose uptake by yeast cells. Hence, the in vivo antidiabetic screening was done for these six compounds. Among all six T1, T7, T13 showed significant blood glucose level decrease compared to standard pioglitazone HCl. Also T1, T7 and T13 showed better antioxidant activity with lower IC50 value than standard ascorbic acid, and hence in vivo cardioprotective studies were done for these. The ECG studies showed that T1 (SSDMA1) and T7 (SSDMA13) were better effective than SDMA49 (T13) in restoring the normal functioning of the heart, thus may help in preventing the development of diabetic cardiomyopathy (DCM) and controlling T2DM.

Diversity of Secondary Structure in Catalytic Peptides with β-Turn-Biased Sequences

X-ray crystallography has been applied to the structural analysis of a series of tetrapeptides that were previously assessed for catalytic activity in an atroposelective bromination reaction. Common to the series is a central Pro-Xaa sequence, where Pro is either l- or d-proline, which was chosen to favor nucleation of canonical β-turn secondary structures. Crystallographic analysis of 35 different peptide sequences revealed a range of conformational states. The observed differences appear not only in cases where the Pro-Xaa loop-region is altered, but also when seemingly subtle alterations to the flanking residues are introduced. In many instances, distinct conformers of the same sequence were observed, either as symmetry-independent molecules within the same unit cell or as polymorphs. Computational studies using DFT provided additional insight into the analysis of solid-state structural features. Select X-ray crystal structures were compared to the corresponding solution structures derived from measured proton chemical shifts, 3J-values, and 1H-1H-NOESY contacts. hese findings imply that the conformational space available to simple peptide-based catalysts is more diverse than precedent might suggest. The direct observation of multiple ground state conformations for peptides of this family, as well as the dynamic processes associated with conformational equilibria, underscore not only the challenge of designing peptide-based catalysts, but also the difficulty in predicting their accessible transition states. These findings implicate the advantages of low-barrier interconversions between conformations of peptide-based catalysts for multistep, enantioselective reactions.

Cyclic dipeptides exhibit potency for scavenging radicals

Twenty kinds of cyclic dipeptides containing l-leucine were synthesized, and their antioxidant activity against .OH and O2·- was investigated. Compounds possessing polar amino acid residues, such as Asp, Cys, Glu, Lys, Pro, Ser, and Trp, exhibited higher antioxidant activity against .OH than vitamin E. However, only cyclo(l-Cys-l-Leu) scavenged O2·-.

2-Benzoyl-2-ethoxycarbonylvinyl-l and 2-Benzoylamino-2-methoxy-carbonylvinyl-1 as N-Protecting Groups in Peptide Synthesis. Their Application in the Synthesis of Dehydropeptide Derivatives Containing N-Terminal 3-Heteroarylamino-2,3-dehydroalanine

Ethyl 2-benzoyl-3-dimethylaminopropenoate (6) and methyl 2-benzoylamino-3-dimethylaminopropenoate (46) were used as reagents for the protection of the amino group with 2-benzoyl-2-ethoxycarbonylvinyl-1 and 2-benzoylamino-2-methoxycarbonylvinyl groups in t

Pyroglutamyl-histidyl-tryptophanyl-seryl-tyrosyl hydrazides

A new decapeptide having the formula, pGlu-His-Trp-Ser-Tyr-Gly-Leu-NO2 Arg-Pro-Gly(NH2); salts thereof; production thereof by reacting pGlu-His-Trp-Ser-Tyr(N3) with Gly-Leu-NO2 Arg-Pro-Gly(NH2), by reacting pGlu-His-Trp-Ser-Tyr-Gly(N3) with Leu-NO2 Arg-Pro-Gly(NH2), or by reacting pGlu-His-Trp-Ser-Tyr-Gly-Leu(N3) with NO2 Arg-Pro-Gly(NH2); certain peptide intermediates and their salts used in the production thereof; and the use thereof in the preparation of luteinizing hormone releasing factor.