Amino Acids

• Introduction
• Application
• Case Study
• Research Articles

Introduction

Amino acids are important organic components of proteins, which are essential macromolecules in all living organisms. They play vital roles in a variety of biological processes, including enzyme function, cell signaling, structural support, and molecular transport. There are 20 standard amino acids commonly found in proteins. These amino acids are distinguished by their side chains (R groups), giving each amino acid unique chemical properties.

Alfa Chemistry offers its customers a wide range of high-quality amino acids. Whether you are a researcher, scientist or health enthusiast, we offer a range of amino acids to meet your specific needs.

Explore our range below:

Alfa Chemistry offers the following standard amino acids:

• Glycine (Gly)
• Alanine (Ala)
• Valine (Val)
• Leucine (Leu)
• Isoleucine (Ile)
• Glutamic acid (Glu)
• Histidine (His)

• Tryptophan (Trp)
• Serine (Ser)
• Threonine (Thr)
• Cysteine (Cys)
• Asparagine (Asn)
• Aspartic acid (Asp)

• Methionine (Met)
• Phenylalanine (Phe)
• Tyrosine (Tyr)
• Glutamine (Gln)
• Lysine (Lys)
• Arginine (Arg)

Unusual Amino Acids Available from Alfa Chemistry

Non-standard amino acids are "non-proteinogenic" because they are not genetically encoded or incorporated during translation. Non-natural amino acids can enhance the stability or functionality of a therapeutic target and can be site-specifically incorporated into synthetic custom peptides.

Alfa Chemistry offers non-standard amino acids, including analogs, modified amino acids, specially functionalized structural units, polyethylene glycolated amino acids, and more, suitable for various research applications, including post-translational modifications.

Amino acid analogs	Functional unnatural amino acids
Alanine, glycine, valine and leucine analogs Arginine and lysine analogs Aspartic acid and glutamate analogues Cysteine and methionine analogs Phenylalanine and tyrosine analogs proline analogs Serine, threonine and statin analogs tryptophan analogs	Azide and alkyne building blocks Acetylated amino acids Glycosylated amino acids Methylated amino acids Phosphorylated amino acids binding building blocks dye-labeled amino acids PEGylated amino acids and special linkers N-alpha-methylamino acid β-amino acid Heterocyclic amino acids

Applications

• Protein research: amino acids are essential for studying protein structure, function, and interactions.
• Biotechnology: amino acids are used in the production of recombinant proteins, antibodies, and enzymes.
• Nutritional supplements: amino acids are used to formulate dietary supplements to support muscle growth, recovery, and overall health.
• Pharmaceuticals: Amino acids play a vital role in the development of drugs and therapies.
• Cosmetics and Personal Care: Certain amino acids are added to skin and hair care products for their beneficial properties.

Browse our range of organic building blocks/amino acids today and unlock the potential of these important molecular components!

Case Study

How Does Serine Reduce Oxidative Stress?

Zhou X, et al. Molecular Nutrition & Food Research, 2017, 61(11), 1700262.

Serine is metabolically indispensable because it is located at a key node connecting the biosynthetic flow from glycolysis to purine synthesis, the one-carbon metabolic cycle, and glutathione synthesis. The antioxidant function of serine and its related mechanisms were studied using diquat as an effective chemical agent for inducing oxidative stress. Results indicate that L-serine supplementation alleviates hepatic oxidative stress by improving the synthesis of glutathione as its substrate, and by supporting methionine cycle as a one-carbon unit supplier.
Experimental Design
• All experimental mice were randomly assigned into five groups (n=10): 1) control (CON); 2) diquat (DIQ); 3) diquat + 0.1% (wt:vol) serine (LS); 4) diquat + 0.5% serine (MS); 5) diquat + 1% serine (HS).
• L-serine was supplemented in the drinking water at concentrations of 0.1%, 0.5% and 1% (wt/vol), respectively. All mice except control were injected intraperitoneally with diquat at 24 mg/kg body weight after 14 days.
• Then blood was taken from the retro-orbital sinus 3 h after the injection and liver samples were collected for further analysis after mice were killed by cervical dislocation.

Synthetic Route of Lysine-Assisted Palladium Nanochain Networks

Yang G, et al. Chemical Engineering Journal, 2020, 379, 122230.

An efficient route to synthesize palladium nanochain networks (Pd NCNs) with the help of lysine molecules and polyvinylpyrrolidone (PVP) protection was developed. The prepared Pd NCNs exhibit excellent electrocatalytic activity and oxygen reduction reaction (ORR) stability in neutral media, which means its application potential in microbial fuel cells (MFC).
Controlled synthesis of Pd nanochains by lysine
• Pd NCNs were typically prepared as follows: 0.5 mL of 0.05 M PdCl₂ solution, 2.0 mL of lysine solution(0.05 M), and 50 mg of PVP (MW=30,000) were mixed with 6.0 mL of deionized water under continuous stirring for 10 min at a temperature of 296 ±5 K.
• After the pH was adjusted to 12.0, the solution was transferred to a Teflon-lined stainless-steel autoclave with a volume of 20 mL and was heated at 413 K for 3 h. After being cooled to room temperature, the obtained Pd NCNs were centrifugated, washed several times with water, and then dried at 333K under vacuum for 5 h.
• Finally, before electrochemical tests, the Pd NCNs were treated by UV irradiation with wavelengths of 185 and 254 nm in air for 4 h to remove the capping agent.

Simulation Study on Bioferroelectric Properties of Glycine Crystals

Hu, Pengfei, et al. The Journal of Physical Chemistry Letters, 2019, 10(6), 1319-1324.

Glycine, a fundamental component of biological structures, has been found to possess nanoscale ferroelectric properties. Under ambient conditions, glycine crystals mainly exist in the α-, β-, or γ-phase. Using first-principles density functional theory (DFT) calculations and molecular dynamics (MD) simulations, the ferroelectric properties of glycine crystals can be elucidated, including equilibrium polarization and dynamic phase transition mechanisms. The results show that glycine crystals can produce larger polarization than traditional inorganic ferroelectrics, and glycine exhibits good ferroelectric properties. This means that the biocompatibility and ferroelectricity of glycine crystals will make them promising candidates for biomedical applications.
Bioferroelectric properties of glycine crystals
• The ferroelectricity of β-glycine originates from the ordered arrangement of -NH³⁺ groups, resulting in a weak ferroelectric arrangement. For polarization along the b-axis, the -NH³⁺ group undergoes a transition from a paraelectric structure to a ferroelectric structure.
• The polarization of the two γ-glycine phases is approximately five times greater than that of the β-glycine phase and is similar to that of conventional ferroelectric materials. In γ-glycine, the moments are arranged in a helix with the net component along the c-axis. γ-Glycine should have a spontaneous polarization of approximately 70.9 μC·cm^-2 at 300 K.
• System MD simulations were performed using polarized crystal charges (PCC) based on protein-specific polarized charges (PPC). The Curie temperature of γ-glycine is 630 K and the coercive field required to switch its polarized state is 1 V· nm^–1.

Tyrosine for Assisted Size-Controlled Synthesis of Silver Nanoparticles

Maddinedi S B, et al. Environmental Toxicology and Pharmacology, 2017, 51, 23-29.

Tyrosine can be used as a reducing agent and capping agent to prepare size-controlled silver nanoparticles (SNPs). By changing the pH of the tyrosine solution, control of SNP size can be achieved simply and effectively. The prepared tyrosine-terminated silver nanocolloids possess catalytic activity for the reduction of 4-nitrophenol, and their catalytic activity depends on the size of the nanoparticles.
Synthesis and catalytic activity evaluation of tyrosine-capped SNPs
• To prepare SNPs of different sizes, 9 mL of the L-tyrosine (1mM) solutions of different pH (10, 11 and 12) were added to 10 mL of AgNO₃ (1mM) solution in different test tubes.
• Then, the reaction mixture was heated at 90℃ for 30 min. The change in colour of the reaction solutions from colorless to light yellow or brown indicated the formation of SNPs.
• In order to study the comparative catalytic activity of the SNPs of different sizes, a suitable amount of SNPs were added to the reaction mixture of 1mL of NaBH₄ (0.1 M) and 1.9 mL of 4-NP (1 mM) solution. The gradual change in color of the solution from deep yellow to colorless indicated the 4-NP reduction.
• The whole reaction was performed in quartz cuvette and the optical absorbance was monitored by using the UV-Visible spectroscopy.

Research Articles

Carbon Isotope Labeling of Amino Acids by CO₂ Carboxylic Acid Exchange