3918-94-3

Basic information

• Product Name: H-VAL-VAL-OH
• Synonyms: VAL-VAL;L-VALYL-L-VALINE;L-VAL-VAL;H-VAL-VAL-OH;valylvaline;L-Val-L-Val-OH;L-Val-Val-OH;N-Valyl-L-valine
• CAS NO: 3918-94-3
• Molecular Formula: C₁₀H₂₀N₂O₃
• Molecular Weight: 216.28
• Mol File: 3918-94-3.mol
• Article Data: 18

Chemical Properties

• Melting Point: 253-254 °C(Solv: ethanol (64-17-5))
• Boiling Point: 411.6°C at 760 mmHg
• Flash Point: 202.7°C
• Appearance: /
• Density: 1.084g/cm³
• Vapor Pressure: 6.29E-08mmHg at 25°C
• Refractive Index: 1.483
• Storage Temp.: −20°C
• PKA: 3.16±0.10(Predicted)
• CAS DataBase Reference: H-VAL-VAL-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-VAL-VAL-OH(3918-94-3)
• EPA Substance Registry System: H-VAL-VAL-OH(3918-94-3)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 3918-94-3(Hazardous Substances Data)

Usage

Description

H-VAL-VAL-OH, also known as a dipeptide of the amino acid valine, is a compound consisting of two L-valine residues connected by a peptide bond. Valine is an essential amino acid that is not synthesized in the body and must be obtained through dietary sources such as beans, dairy products, and soy products. This dipeptide has potential applications in various industries due to its unique properties and the nutritional benefits of valine.

Uses

Used in Pharmaceutical Industry:
H-VAL-VAL-OH is used as a pharmaceutical compound for its potential therapeutic applications. The dipeptide may be utilized in the development of drugs targeting specific conditions, as it can be modified and combined with other molecules to enhance its bioactivity and specificity.
Used in Nutritional Supplements:
H-VAL-VAL-OH is used as an ingredient in nutritional supplements for its valine content. Valine plays a crucial role in muscle metabolism, tissue repair, and energy production. As a dipeptide, it may have improved bioavailability and absorption compared to individual amino acids, making it a valuable addition to supplements targeting muscle growth, recovery, and overall health.
Used in Sports Nutrition:
In the sports nutrition industry, H-VAL-VAL-OH is used as a component in products designed to support muscle growth, endurance, and recovery. The dipeptide's valine content may contribute to these effects, as valine is known to be particularly important for muscle tissue repair and energy production during exercise.
Used in Food and Beverage Industry:
H-VAL-VAL-OH can be used as an additive in the food and beverage industry to enhance the nutritional profile of products. Its valine content may provide an additional source of this essential amino acid, which can be beneficial for consumers seeking to increase their protein intake or improve the overall quality of their diet.
Used in Cosmetics Industry:
In the cosmetics industry, H-VAL-VAL-OH may be used as an ingredient in skincare and hair care products due to its potential benefits for skin and hair health. Valine is known to play a role in collagen synthesis, which is important for maintaining skin elasticity and strength. Additionally, the dipeptide may contribute to hair growth and repair by providing a source of essential amino acids for keratin production.

InChI:InChI=1/C10H20N2O3/c1-5(2)7(11)9(13)12-8(6(3)4)10(14)15/h5-8H,11H2,1-4H3,(H,12,13)(H,14,15)

Upstream product

• 19542-54-2 N-benzyloxycarbonyl-L-valyl-L-valine 
• 6306-50-9 N-(N,N-phthaloyl-L-valyl)-L-valine 
• 24733-24-2 Pipoc-Val-Val 
• 35761-09-2 Cbz-L-val-L-val-Cbz 
• 26993-93-1 N-Benzyloxycarbonyl-L-valyl-L-valin-4-methoxybenzylester 
• 40719-51-5 N-[(S)-3-methyl-2-(2-oxo-4,5-diphenyl-oxazol-3-yl)-butyryl]-L-valine methyl ester 
• 69209-72-9 (N-tert-butoxycarbonyl-L-valyl)-L-valine 
• 101222-19-9 L-Valyl-L-valine benzyl ester 
• 77443-49-3 (S)-benzyl 2-((S)-2-((tert-butoxycarbonyl)amino)-3-methylbutanamido)-3-methylbutanoate 
• 13734-41-3 t-Boc-L-valine 
• 72-18-4 L-valine 
• 112-80-1 cis-Octadecenoic acid 
• 24601-74-9 (S)-4-isopropyloxazolidine-2,5-dione 
• 124-07-2 Octanoic acid 

Downstream Products

• 79672-11-0 N-(N-glycyl-L-valyl)-L-valine 
• 19943-16-9 (3S,6S)-3,6-bis(isopropyl)piperazine-2,5-dione 
• 134806-73-8 5-[(S)-1-((S)-1-Carboxy-2-methyl-propylcarbamoyl)-2-methyl-propylcarbamoyl]-pentanoic acid methyl ester 
• 402958-47-8 (S)-3-Methyl-2-((S)-3-methyl-2-{5-[1-(1-methyl-1-phenyl-ethyl)-1H-tetrazol-5-yl]-pentanoylamino}-butyrylamino)-butyric acid 
• 69936-04-5 (+)-(S)-valyl-(S)-valine methyl ester hydrochloride 
• 132847-82-6 (3S,6S,12S,15S)-3,6,12,15-Tetraisopropyl-1,10-dioxa-4,7,13,16-tetraaza-cyclooctadecane-2,5,8,11,14,17-hexaone 
• 306314-21-6 (3S,4R)-5,5,5-Trifluoro-3-hydroxy-4-[(S)-2-((3S,4R)-5,5,5-trifluoro-3-hydroxy-4-{(S)-3-methyl-2-[(S)-3-methyl-2-(3-methyl-butyrylamino)-butyrylamino]-butyrylamino}-pentanoylamino)-propionylamino]-pentanoic acid methyl ester 
• 408349-66-6 N-{(S)-1-[(S)-1-(2,3-Dihydroxy-benzylcarbamoyl)-2-methyl-propylcarbamoyl]-2-methyl-propyl}-2,3-dihydroxy-benzamide 
• 408349-49-5 N-{(S)-1-[(S)-1-(2,3-Dimethoxy-benzylcarbamoyl)-2-methyl-propylcarbamoyl]-2-methyl-propyl}-2,3-dimethoxy-benzamide 
• 188054-60-6 (1-{1-[1-[3-cyano-1-ethyl-2-oxo-3-(triphenyl-λ⁵-phosphanylidene)-propylcarbamoyl]-2-methylpropylcarbamoyl]-2-methylpropylcarbamoyl}-2-methylpropyl)-carbamic acid benzyl ester 
• 135219-43-1 2-(2-{3-[2-(2-amino-3-methylbutyrylamino)-3-methyl-butyrylamino]-2-oxo-pentanoylamino}-4-methylpentanoylamino)-3-methylbutyric acid 

Relevant articles and documents

Effect of high hydrostatic pressure on prebiotic peptide synthesis

Prebiotic peptide synthesis is a central issue concerning life's origins. Many studies considered that life might come from Hadean deep-sea environment, that is, under high hydrostatic pressure conditions. However, the properties of prebiotic peptide formation under high hydrostatic pressure conditions have seldom been mentioned. Here we report that the yields of dipeptides increase with raised pressures. Significantly, effect of pressure on the formation of dipeptide was obvious at relatively low temperature. Considering that the deep sea is of high hydrostatic pressure, the pressure may serve as one of the key factors in prebiotic peptide synthesis in the Hadean deep-sea environment. The high hydrostatic pressure should be considered as one of the significant factors in studying the origin of life.

An efficient and cost-effective approach to kahalalide F N-terminal modifications using a nuisance algal bloom of Bryopsis pennata

Background: Kahalalide F (KF) and its isomer iso-kahalalide F (isoKF), both of which can be isolated from the mollusk Elysia rufescens and its diet alga Bryopsis pennata, are potent cytotoxic agents that have advanced through five clinical trials. Due to a short half-life, narrow spectrum of activity, and a modest response in patients, further efforts to modify the molecule are required to address its limitations. In addition, due to the high cost in producing KF analogues using solid phase peptide synthesis (SPPS), a degradation and reconstruction approach was employed using natural KF from a seasonal algal bloom to generate KF analogues. Methods: N-protected KF was carefully hydrolyzed at the amide linkage between L-Thr12 and D-Val13 using dilute HCl. The synthesis of the C-terminal fragment began with the formation of hexanoic succinimide ester, followed by a reaction with dipeptides. The final coupling reaction was performed between the semisynthesized Fmoc-KF hydrolysis product and the C-terminal fragment, followed by the deprotection of the Fmoc group. Results: Six KF analogues with an addition of an amino acid residue on the N-terminal chain, D-Val14-isoKF (2), Val13-Val14-isoKF (3), D-Leu14-isoKF (4), D-Pro14-isoKF (5), D-Phe14-isoKF (6), and 3,4-2F-D-Phe14-isoKF (7) were prepared using semisynthesis at the exposed N-terminal chain. Conclusions: The overall yield of the medication was 45%. This approach is economical, efficient and amendable to large-scale production while eliminated a nuisance algal bloom. General significance: B. pennata blooms are capable of producing KF in good yields. The semisynthesis from the natural product produced N-terminal modifications for the construction of inexpensive semisynthetic KF libraries.

A novel L-amino acid ligase from bacillus subtilis NBRC3134 catalyzed oligopeptide synthesis

L-Amino acid ligase catalyzes dipeptide synthesis from unprotected L-amino acids in an ATP-dependent manner. We have purified a new L-amino acid ligase, RizA, which synthesizes dipeptides whose N-terminus is Arg, from Bacillus subtilis NBRC3134, a microorganism that produces a rhizocticin peptide antibiotic. It was suggested that RizA is probably involved in rhizocticin biosynthesis. In this study, we performed sequence analysis of unknown regions around rizA, and newly identified a gene that encodes a protein that possesses an ATP-grasp motif upstream of rizA. This gene was designated rizB, and its recombinant protein was prepared. Recombinant RizB synthesized homo-oligo-mers of branched-chain L-amino acids and L-methionine consisting of two to five amino acids in an ATP-dependent manner. RizB also synthesized various heteropeptides. Further examination showed that RizB might elongate a peptide chain at the N-terminus. This is the first report on an L-amino acid ligase catalyzing oligopeptide synthesis.