7763-65-7

Basic information

• Product Name: H-HIS-LEU-OH
• Synonyms: (S)-2-((S)-2-aMino-3-(1H-iMidazol-4-yl)propanaMido)-4-Methylpentanoic acid;L-Leucine, L-histidyl-;N-Histidylleucine;-2-Amino-3-(1H-imidazol-4-yl);His-Leu-OH≥ 99% (TLC);L-HISTIDYL-L-LEUCINE;H-HIS-LEU-OH;HIS-LEU
• CAS NO: 7763-65-7
• Molecular Formula: C₁₂H₂₀N₄O₃
• Molecular Weight: 268.31
• Product Categories: Dipeptides;Dipeptides and Tripeptides;Peptides
• Mol File: 7763-65-7.mol

Chemical Properties

• Melting Point: 217-220℃
• Boiling Point: 623 °C at 760 mmHg
• Flash Point: 330.6 °C
• Appearance: /
• Density: 1.249 g/cm³
• Vapor Pressure: 2.21E-16mmHg at 25°C
• Refractive Index: 1.559
• Storage Temp.: −20°C
• CAS DataBase Reference: H-HIS-LEU-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-HIS-LEU-OH(7763-65-7)
• EPA Substance Registry System: H-HIS-LEU-OH(7763-65-7)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 7763-65-7(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
H-HIS-LEU-OH is used as a pharmaceutical compound for its potential therapeutic effects. The dipeptide structure allows it to interact with various biological targets, making it a promising candidate for the development of new drugs.
Used in Nutritional Supplements:
In the field of nutrition, H-HIS-LEU-OH can be used as an ingredient in dietary supplements, providing essential amino acids to support muscle growth, repair, and overall health.
Used in Cosmetics Industry:
H-HIS-LEU-OH may also find applications in the cosmetics industry, where it can be used as an active ingredient in skincare products to promote skin health and improve the appearance of the skin.
Used in Research and Development:
In the research and development sector, H-HIS-LEU-OH can be utilized as a building block for the synthesis of more complex peptides and proteins, contributing to the advancement of biotechnology and pharmaceutical innovations.
Used in Food Industry:
H-HIS-LEU-OH can be employed in the food industry as a flavor enhancer or as a component in the development of novel food products with improved nutritional profiles.

InChI:InChI=1/C12H20N4O3/c1-7(2)3-10(12(18)19)16-11(17)9(13)4-8-5-14-6-15-8/h5-7,9-10H,3-4,13H2,1-2H3,(H,14,15)(H,16,17)(H,18,19)

Upstream product

• 106654-30-2 N-(1,N^α-bis-benzyloxycarbonyl-histidyl)-leucine methyl ester 
• 122338-83-4 N-(1-benzyl-N^α-benzyloxycarbonyl-L-histidyl)-L-leucine-benzyl ester 
• 2743-60-4 L-Leucine ethyl ester 
• 18428-28-9 N-cyclohexylcarbodiimide 
• 74853-62-6 N^α,N^im-ditritylhistidine 
• 38972-90-6 N-(N^α-benzyloxycarbonyl-histidyl)-leucine 
• 30033-84-2 N-(N^α-benzyloxycarbonyl-histidyl)-leucine methyl ester 
• 41445-69-6 N-benzyloxycarbonyl-L-histidyl azide 
• 77422-47-0 (S)-2-{(S)-2-tert-Butoxycarbonylamino-3-[1-(diphenyl-pyridin-4-yl-methyl)-1H-imidazol-4-yl]-propionylamino}-4-methyl-pentanoic acid methyl ester 
• 77422-41-4 (S)-2-{(S)-2-tert-Butoxycarbonylamino-3-[1-(diphenyl-pyridin-4-yl-methyl)-1H-imidazol-4-yl]-propionylamino}-4-methyl-pentanoic acid 
• 64991-62-4 N(α)-t-butoxycarbonyl-N(Im)-diphenyl-4-pyridylmethyl-L-histidine 
• 2666-93-5 (S)-Leu-OMe 
• 484-42-4 angiotensin I 
• 31373-65-6 N-α-hippuryl-L-histidyl-L-leucine 

Downstream Products

• 31373-65-6 N-α-hippuryl-L-histidyl-L-leucine 
• 1093075-61-6 histidinylleucinato^(2-)-O,N,N-diphenyltin(IV) 

Relevant articles and documents

A study of chimeras constructed with the two domains of angiotensin I-converting enzyme

Angiotensin I-converting enzyme (ACE) is composed of two highly similar domains called the N and C domains, which display some contrasting enzymatic properties. We constructed two ACE chimeras: chimera 1, comprised of the N domain containing the central 60 amino acid residues of the C domain, and chimera 2, comprised of the C domain containing the central 60 amino acid residues of the N domain. Chimeras 1 and 2 displayed K(m) values for Hip-His-Leu and Z-Phe-His-Leu and k(cat) ratios for these two substrates similar to that of the N and C domains, respectively. Thus, the short sequence exchanged between the two domains does not confer the specific properties of that domain for these two substrates but, rather, such specific properties must arise from the sequences surrounding the central region in each domain.

Structural and Functional Peculiarities of Homologous Domains of Angiotensin-Converting Enzyme

Somatic angiotensin-converting enzyme (ACE) consists of two homologous domains, each of them containing an active site. Differences in substrate specificities and affinity to inhibitors of the active sites of the two domains of bovine ACE are described. The ACE domains demonstrate different thermostability, and the reasons for this difference are analyzed. A structural model of the ACE domains is suggested, which allows us to reveal the structural subdomain important for the protein stability and localize the hydrophobic and carbohydrate-binding sites.

DPP4 INHIBITOR AND PHARMACEUTICAL APPLICATION THEREOF

The present invention provides a Dpp4 inhibitor which comprises a leucine derivative of the following formula (1) or a methionine derivative of the following formula (2): wherein each R1 and R3 represents a hydrogen atom (H) and an L-amino acid residue; R2 represents a hydroxyl group (OH), alkoxy group having 1 to 6 carbon atoms, amino group (NH2), alkylamino group having 1 to 6 carbon atoms, glycine residue, β-alanine residue, L-amino acid (except for proline, alanine and phenylalanine) residue or L-amino-acid amide (except for proline amide, alanine amide and phenylalanine amide) residue; and R4 represents a hydroxyl group (OH), alkoxy group having 1 to 6 carbon atoms, amino group (NH2), alkylamino group having 1 to 6 carbon atoms, glycine residue, β-alanine residue, L-amino acid (except for proline and alanine) residue or L-amino-acid amide (except for proline amide and alanine amide) residue. These derivatives also act as autophagy regulators.

The molecular basis for the selection of captopril cis and trans conformations by angiotensin I converting enzyme

Enzyme-inhibitor recognition is considered one of the most fundamental aspects in the area of drug discovery. However, the molecular mechanism of this recognition process (induced fit or prebinding and adaptive selection among multiple conformers) in several cases remains unexplored. In order to shed light toward this step of the recognition process in the case of human angiotensin I converting enzyme (hACE) and its inhibitor captopril, we have established a novel combinatorial approach exploiting solution NMR, flexible docking calculations, mutagenesis, and enzymatic studies. We provide evidence that an equimolar ratio of the cis and trans states of captopril exists in solution and that the enzyme selects only the trans state of the inhibitor that presents architectural and stereoelectronic complementarity with its substrate binding groove.

Amino-acids and Peptides. Part 45. The Protection of the Thiol Function of Cysteine and the Imidazole-N of Histidine by the Diphenyl-4-pyridylmethyl Group

S-(Diphenyl-4-pyridylmethyl)-L-cysteine (1) and its derivatives (2)-(7) have been prepared and used in peptide synthesis.In contrast to the analogous S-trityl group, this protection is stable in acid but it is cleaved readily by zinc-acetic acid, by mercury(II) acetate, by iodine, and by electrolytic reduction.N(Im)-Diphenyl-4-pyridylmethyl-L-histidine derivatives (9)-(13) are also reported; the protecting group is again stable to acid but cleaved by hydrogenolysis, by zinc-acetic acid, and by electrolytic reduction, and it has been used in the synthesis of L-histidyl-L-leucine, -L-phenylalanine, and -glycine.