Arginine

Catalog Number	ACM74793-7
CAS	74-79-3
Structure
Description	Arginine is an amino acid, which is one of the building blocks of proteins. It is classified as a semi-essential or conditionally essential amino acid, meaning that under certain circumstances, such as during growth or illness, the body may not be able to produce enough arginine and it must be obtained from the diet. Arginine has numerous biological functions in the body, including contributing to immune function, wound healing, hormone secretion, and blood flow regulation.
Synonyms	L-Arginine
IUPAC Name	(2S)-2-amino-5-(diaminomethylideneamino)pentanoic acid
Molecular Weight	174.2
Molecular Formula	C6H14N4O2
Canonical SMILES	C(C[C@@H](C(=O)O)N)CN=C(N)N
InChI	ODKSFYDXXFIFQN-BYPYZUCNSA-N
InChI Key	InChI=1S/C6H14N4O2/c7-4(5(11)12)2-1-3-10-6(8)9/h4H,1-3,7H2,(H,11,12)(H4,8,9,10)/t4-/m0/s1
Boiling Point	305°C
Melting Point	222 °C (dec.) (lit.)
Purity	99%+
Density	1.23g/ml
Appearance	white, crystalline powder that is water-soluble and odorless
Application	1. Helps improve blood flow and circulation 2. Enhances athletic performance and endurance 3. Boosts immune system function 4. Supports wound healing and tissue repair 5. May aid in erectile dysfunction by improving blood flow to the genitals 6. Assists in reducing high blood pressure 7. Can act as a natural remedy for migraines and headaches by dilating blood vessels 8. May have anti-aging effects due to its role in collagen production.
Complexity	176
Covalently-Bonded Unit Count	1
Defined Atom Stereocenter Count	1
Exact Mass	174.1116757
Heavy Atom Count	12
Hydrogen Bond Acceptor Count	4
Hydrogen Bond Donor Count	4
Isomeric SMILES	C(C[C@@H](C(=O)O)N)CN=C(N)N
Monoisotopic Mass	174.1116757
pH	10.5-12.0 (0.5M, H2O, 25°C)
Physical State	Solid
Rotatable Bond Count	5
Topological Polar Surface Area	128 Ų

Knowledge & Learning Case Study Q&A

The Role of Arginine in Polymyxin-Dependent Acinetobacter baumannii

Han M-L, et al. Cell Reports, 2024, 43(7), 114410.

Polymyxins are critical antibiotics effective against the "Critical" pathogen Acinetobacter baumannii. However, the emergence of highly polymyxin-resistant A. baumannii strains that depend on polymyxins for survival has posed significant challenges in clinical diagnosis and treatment. This study investigates the essential role of arginine metabolism in polymyxin-dependent A. baumannii, providing insights into the molecular mechanisms and potential strategies for improving diagnosis and treatment.
The arginine degradation pathway is significantly altered in polymyxin-dependent A. baumannii strains compared to wild-type strains. Key metabolites such as L-arginine and L-glutamate are depleted, and the expression of the astABCDE operon is significantly increased. This operon encodes enzymes in the arginine succinyltransferase (AST) pathway, which converts arginine to glutamate, serving as a major source of carbon, nitrogen, and energy.
Arginine Supplementation
Supplementing arginine enhances bacterial metabolic activity and suppresses polymyxin dependence. Deletion of astA, the first gene in the arginine degradation pathway, leads to decreased phosphatidylglycerol and increased phosphatidylethanolamine levels in the outer membrane, reducing interactions with polymyxins. This indicates that arginine plays a crucial role in stabilizing the outer membrane and decreasing oxidative stress, which is essential for the survival of polymyxin-dependent strains.
Metabolomics analysis showed significant depletion of metabolites involved in arginine biosynthesis and degradation in polymyxin-dependent strains, with levels restored in the presence of colistin. This emphasizes the importance of arginine in bacterial growth and reducing polymyxin dependence.
Lysine Interaction
Lysine, another amino acid, also plays a role in improving the diagnosis of polymyxin-dependent bacteria. Both lysine and arginine can bind to the same proteins, such as ArgT, ArgO, and ArgP, further highlighting the significance of arginine metabolism in enhancing bacterial diagnostics.

Arginine for the Development of Novel Photodynamic Inactivation Systems

Wang JJ, et al. International Journal of Food Microbiology, 2015, 411, 110539.

L-Arginine (L-Arg) and curcumin (Cur) exhibit synergistic bactericidal effects, making them promising candidates for the development of novel curcumin-mediated photodynamic inactivation (PDI) systems. These systems leverage the combined properties of L-Arg and Cur to enhance bactericidal efficacy against food-borne pathogens like Vibrio parahaemolyticus. The combination of L-arginine and curcumin in a photodynamic inactivation system offers a potent approach to controlling microbial growth in seafood.
Mechanism of Action: The synergistic effect between curcumin and L-arginine significantly enhances the inactivation of Vibrio parahaemolyticus. L-arginine disrupts the bacterial membrane structure and iron homeostasis through its metal-chelating abilities and strong interactions with phospholipids. This disruption facilitates the penetration of curcumin into the bacterial cell, where it binds to DNA, interrupting replication and protein synthesis. The combined action leads to the conversion of reactive oxygen species (ROS) into reactive nitrogen species (RNS), resulting in a potent bactericidal effect. Additionally, this synergy effectively inhibits pH changes, lipid oxidation, and protein degradation, while preserving the appearance and quality of shrimp during storage.
PDI Treatment Protocol
Preparation: Bacterial suspensions were prepared with varying concentrations of curcumin and L-Arg.
Incubation: 500 μL of the mixed suspension was added to a 24-well plate.
Irradiation: The samples were irradiated with blue LED light for 5 minutes (1.2 J/cm²).
Assessment: Post-irradiation, 100 μL of the suspension was diluted, plated on TCBS agar, and viable cells were quantified (Log CFU/mL).
ROS and RNS Generation
ROS Detection: ROS levels were measured using 2,7-dichlorofluorescin diacetate (DCFH-DA) at 10 μM concentration. The fluorescence signal was monitored at λex/λem = 484/525 nm.
RNS Detection: RNS levels were measured using BBoxiProbe O53 at 8 μM concentration. The fluorescence signal was monitored at λex/λem = 518/606 nm.
NO Release Analysis: Nitric oxide (NO) release was analyzed using the Griess method, with absorbance monitored at OD560 nm.
Application on Shrimp
Inoculation: 100 μL of Vibrio parahaemolyticus suspension (~6.0 Log CFU/g) was inoculated on shrimp and allowed to attach for 20 minutes.
Treatment: The inoculated shrimp were soaked in a suspension containing curcumin and L-Arg for 20 minutes, followed by blue LED irradiation.
Storage and Analysis: Treated samples were stored at 10°C. Post-treatment, shrimp samples were homogenized in 0.85% NaCl, and the supernatant was plated on TCBS agar to determine viable cells.

L-arginine for the Preparation of PVA/HA/L-Arginine Nanofibres for Wound Healing Applications

Hussein Y, et al. International Journal of Biological Macromolecules, 2020, 164, 667-676.

L-arginine can be used to prepare Polyvinyl alcohol (PVA)/hyaluronic acid (HA)/L-arginine nanofibres by electrostatic spinning method and is expected to be used for wound healing.L-arginine can be used as a wound healing accelerator. The addition of cellulose nanocrystals (CNC) to PVA/HA significantly improved the mechanical and swelling properties of NF.
Optimization of Electrospun PVA/HA Nanofibers
PVA (10% w/v) and HA (2% w/v) solutions were prepared separately at room temperature. The solution was then mixed in volume ratios of 50:50, and stirred for 6 hours at 50°C in closed vials to prevent bubble formation and ensure complete homogeneity. CA was added to the polymer solution in varying concentrations. The homogeneous mixture was electrospun using an electrospinner. The polymer solution was loaded into a 5 ml syringe, and electrospinning was performed at flow rates between 0.5 and 1 ml/h, and voltages between 28 and 30 kV. The nanofibers were thermally treated at 100°C for 6 hours. All nanofiber samples were electrospun under ambient conditions with approximately 55% humidity.
Electrospinning of PVA/HA/CNCs and PVA/HA/CNCs/L-Arginine Nanofibrous Scaffolds
CNCs were incorporated as nanofillers in the PVA/HA polymer solution to produce PVA/HA/CNCs nanofibers. 0.25% (w/w) of CNCs was dispersed in a 1.5% CA crosslinked PVA/HA (80:20) solution mixture. After CNC addition, the solutions were stirred at 50°C for 2 hours to achieve a homogeneous and well-dispersed PVA/HA/CNCs blend solution. This mixture was electrospun at 30 kV with a feed rate of 0.5 ml/h, and the PVA/HA/CNCs nanofibers were collected on a static plate collector placed 15 cm from the needle.
To prepare PVA/HA/CNCs/L-arginine nanofibrous scaffolds, 0.26% (w/v) of L-arginine was dissolved in the CA crosslinked PVA/HA/CNCs solution before electrospinning at room temperature. The composite nanofibers were obtained at a voltage of 30 kV, a feed rate of 0.3 ml/h, and a distance of 15 cm.

Arginine for Modification of Chitosan/γ-Polyglutamic Acid Nanoparticles

Su Z, et al. International Journal of Biological Macromolecules, 3021, 168, 215-222

Arginine can be used to prepare a novel nanoparticle (NP) delivery carrier for curcumin based on electrostatic 6-deoxy-6-arginine modified chitosan (DAC) assembled by γ-poly-glutamic acid (γ-PGA). 6-deoxy-6-arginine modified chitosan (DAC) is a water-soluble chitosan derivative with a strong negative charge. A guanidine group is introduced at the C6 position, which gives it some unique properties, such as solubility in neutral and alkaline solutions and stronger antibacterial effect than chitosan.
Preparation of DAC Solution
Chitosan was Schiff-base treated with benzaldehyde as raw material, and the C6 hydroxyl group of the Schiff-base treated chitosan was replaced with p-toluenesulfonyl chloride. The p-toluenesulfonyl group was removed under alkaline conditions, and arginine was added at the C6 position to remove the benzaldehyde protection to obtain DAC.
DAC (50 mg) or γ-PGA was dissolved in 50 mL of water and stirred at 500 r/min for 30 minutes until completely dissolved. Curcumin was dispersed in anhydrous ethanol and stirred overnight in the dark to prepare a 1 mg/mL curcumin solution. As needed, these biopolymer raw material solutions were adjusted to the final pH value and concentration with buffer or ethanol.
Preparation of DAC/γ-PGA Nanoparticles
A 1 mg/mL γ-PGA aqueous solution was added dropwise to a 1 mg/mL DAC solution, and the mixture was stirred at 650 r/min for 60 minutes to allow DAC and γ-PGA to complex via electrostatic interaction. The volume ratio of the mixture (DAC:γ-PGA) ranged from 9:1 to 1:9, with a constant total volume of 10 mL. Nanoparticles were obtained by centrifugation, and the precipitate was washed with distilled water and ethanol. The product was then freeze-dried for subsequent experiments.
To prepare curcumin-loaded nanoparticles, the curcumin solution was added to the γ-PGA aqueous solution, followed by moderate stirring at room temperature for 30 minutes. The preparation then followed the same steps as for non-curcumin-loaded nanoparticles.

How is arginine traditionally obtained?

Arginine is traditionally obtained by hydrolysis of various cheap sources of protein, such as gelatin.

How is arginine commercially produced?

Arginine can be commercially produced by fermentation, using glucose as a carbon source.

How is arginine synthesized in the body?

Arginine is synthesized from citrulline in the urea cycle by the action of argininosuccinate synthetase and argininosuccinate lyase enzymes.

Why is arginine synthesis considered an energetically costly process?

Arginine synthesis is considered energetically costly because for each molecule of argininosuccinate synthesized, one molecule of ATP is hydrolyzed, consuming two ATP equivalents.

How is arginine recycled in the body?

Citrulline, a byproduct of nitric oxide production, can be recycled to arginine in a pathway known as the citrulline to nitric oxide (citrulline-NO) or arginine-citrulline pathway.

What functions does arginine play in the body?

Arginine plays a role in cell division, wound healing, removing ammonia from the body, immune function, and the release of hormones. It is also a precursor for the synthesis of nitric oxide, which regulates blood pressure.

Where is arginine typically found in proteins?

Arginine is typically found on the outside of proteins, where the hydrophilic head group can interact with the polar environment.

How is arginine modified in proteins?

Arginine residues in proteins can be deiminated to form citrulline, and can also be methylated by protein methyltransferases.

What are the precursors and products of arginine?

Arginine is a precursor for nitric oxide, urea, ornithine, agmatine, creatine, and polyamines. Asymmetric dimethylarginine (ADMA), a close relative of arginine, inhibits the nitric oxide reaction and is considered a marker for vascular disease.

Our products and services are for research use only and cannot be used for any clinical purposes.

Online Inquiry

Arginine (74-79-3)

Send A Message