3918-94-3

Usage

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 
• 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 
• 69209-72-9 (N-tert-butoxycarbonyl-L-valyl)-L-valine 
• 56-40-6 L-Glycin 
• 1676-85-3 L-Valin-N-carbonsaeureanhydrid 
• 41445-88-9 Z-Val-OCO₂ⁱBu 
• 3496-11-5 2,5-dioxopyrrolidin-1-yl (2S)-2-(((benzyloxy)carbonyl)amino)-3-methylbutanoate 
• 72-18-4 L-valine 
• 24601-74-9 (S)-4-isopropyloxazolidine-2,5-dione 
• 3392-12-9 Boc-Val-ONSu 
• 13734-41-3 t-Boc-L-valine 
• 6306-50-9 N-(N,N-phthaloyl-L-valyl)-L-valine 

Downstream Products

• 19943-16-9 (3S,6S)-3,6-bis(isopropyl)piperazine-2,5-dione 
• 59452-57-2 N-isovaleryl-L-valyl-L-valine 
• 98-10-2 benzenesulfonamide 
• 124-38-9 carbon dioxide 
• 78-84-2 isobutyraldehyde 
• 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 
• 408349-49-5 N-{(S)-1-[(S)-1-(2,3-Dimethoxy-benzylcarbamoyl)-2-methyl-propylcarbamoyl]-2-methyl-propyl}-2,3-dimethoxy-benzamide 
• 408349-66-6 N-{(S)-1-[(S)-1-(2,3-Dihydroxy-benzylcarbamoyl)-2-methyl-propylcarbamoyl]-2-methyl-propyl}-2,3-dihydroxy-benzamide 
• 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 
• 69936-04-5 (+)-(S)-valyl-(S)-valine methyl ester hydrochloride 

Relevant academic research and scientific papers

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.

N-Carboxyanhydride-Mediated Fatty Acylation of Amino Acids and Peptides for Functionalization of Protocell Membranes

Early protocells are likely to have arisen from the self-assembly of RNA, peptide, and lipid molecules that were generated and concentrated within geologically favorable environments on the early Earth. The reactivity of these components in a prebiotic environment that supplied sources of chemical energy could have produced additional species with properties favorable to the emergence of protocells. The geochemically plausible activation of amino acids by carbonyl sulfide has been shown to generate short peptides via the formation of cyclic amino acid N-carboxyanhydrides (NCAs). Here, we show that the polymerization of valine-NCA in the presence of fatty acids yields acylated amino acids and peptides via a mixed anhydride intermediate. Notably, Nα-oleoylarginine, a product of the reaction between arginine and oleic acid in the presence of valine-NCA, partitions spontaneously into vesicle membranes and mediates the association of RNA with the vesicles. Our results suggest a potential mechanism by which activated amino acids could diversify the chemical functionality of fatty acid membranes and colocalize RNA with vesicles during the formation of early protocells.

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.

Synthesis of dipeptides based on valine and threonine

Val-Val, Val-Thr, and Thr-Val dipeptides were synthesized using trifluoroacetyl protecting group. The optical rotations of the products were similar to those of samples synthesized using Boc protection, which indicated the absence of racemization in the course of introduction and removal of trifluoroacetyl protection. Pleiades Publishing, Ltd., 2012.

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.

Mechanism study on the oligomerization of amino acids into peptides by phosphorus trichloride

As treated by phosphorus trichloride, amino acids could oligomerize into polypeptides. Based on the results obtained by 31P-NMR and ESI-MS/MS, a possible reaction mechanism was proposed. The mechanism might undergo a penta-coordinated phosphorus intermediat. The activated amino acid was a five-membered cyclic penta-coordinated phosphorus intermediate. The nucleophilic attack of the amino group from an amino acid or peptide on the carbonyl group of intermediate led to the formation of peptide and released one equivalent dichloride phosphoric acid. The repetition of the reaction sequence generated a series of oligopeptides. Copyright Taylor & Francis Group, LLC.

A mild Boc deprotection and the importance of a free carboxylate

We report a facile and rapid removal of Boc protecting groups using microwave heating in H2O, with deprotection only requiring a free carboxylic acid group in the starting material. Unlike previous approaches, no additional reagents are required.

The small peptide-catalyzed direct asymmetric aldol reaction in water

The asymmetric aldol reaction is a powerful method for forming carbon-carbon bonds. Small peptides with a primary amine as the catalytic residue catalyze asymmetric aqueous aldol reactions between unmodified ketones and aldehydes to furnish the corresponding aldol products with high ees. The high momodularity of the small peptides should enable the construction of several novel catalysts by combinatorial techniques for the aqueous asymmetric aldol reaction. The remarkably high difference in stereoselectivity between the peptide bond-formation was an important step towards the evaluation of asymmetric catalysis and homochilarity.

Direct asymmetric intermolecular aldol reactions catalyzed by amino acids and small peptides

In nature there are at least nineteen different acyclic amino acids that act as the building blocks of poly-peptides and proteins with different functions. Here we report that α-amino acids, β-amino acids, and chiral amines containing primary amine functions catalyze direct asymmetric intermolecular aldol reactions with high enantio-selectivities. Moreover, the amino acids can be combined into highly modular natural and unusual small peptides that also catalyze direct asymmetric intermolecular aldol reactions with high stereoselectivities, to furnish the corre sponding aldol products with up to > 99% ee. Simple amino acids and small peptides can thus catalyze asymmetric aldol reactions with stereoselectivities matching those of natural enzymes that have evolved over billions of years. A small amount of water accelerates the asymmetric aldol reactions catalyzed by amino acids and small peptides, and also increases their stereoselectivities. Notably, small peptides and amino acid tetrazoles were able to catalyze direct asymmetric aldol reactions with high enantioselectivities in water, while the parent amino acids, in stark contrast, furnished nearly racemic products. These results suggest that the prebiotic oligomerization of amino acids to peptides may plausibly have been a link in the evolution of the homochirality of sugars. The mechanism and stereochemistry of the reactions are also discussed.

Small peptides as modular catalysts for the direct asymmetric aldol reaction: Ancient peptides with aldolase enzyme activity

Simple peptides and their analogues having a primary amino group as the catalytic residue mediate the direct asymmetric intermolecular aldol reaction with high stereoselectivity and furnish the corresponding aldol products with up to 99% ee; this intrinsic ability of highly modular peptides may explain the initial molecular evolution of aldolase enzymes. The Royal Society of Chemistry 2005.