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BOC Sciences provides technical articles related to amino acids, peptides, and peptide nucleic acids (PNA).
Amino acids, a class of organic compounds that contain amino and carboxyl groups are one of the many biologically active macromolecules that build biological organisms, and are the basic materials for building cells and repairing tissues. With a variety of special functional groups and diverse structures, amino acids have a wide range of applications in pharmaceutical, food, cosmetic and other fields.
Glutamic acid, a non-essential amino acid, plays a crucial role in numerous biochemical processes. It is commonly recognized for its involvement in protein synthesis, neurotransmission, and metabolism. However, its significance extends beyond biological systems, with its non-natural derivatives serving key roles in various industries, from pharmaceuticals to food production.
Arginine stands out as a multifunctional amino acid with broad applications spanning pharmaceuticals, biotechnology, food, and cosmetics. Its ability to act as a precursor to essential biomolecules, combined with its diverse physical and chemical properties, makes it indispensable in many industrial processes.
Threonine, an essential amino acid, plays a pivotal role in protein synthesis and serves as a precursor for several important biomolecules. It is characterized by its unique hydroxyl group, which imparts distinct properties that are crucial for various biochemical processes, including immune function and gut health.
Isoleucine is one of the essential amino acids vital for human health, playing critical roles in metabolism, muscle tissue repair, and immune function. As an essential amino acid, it must be obtained from external sources, either through diet or supplements, as the human body cannot synthesize it naturally.
Citrulline is a non-essential amino acid generated from ornithine and carbamoyl phosphate in the urea cycle, or as a byproduct of arginine through nitric oxide synthase (NOS) catalysis. It exists in two forms: the naturally occurring isomer L-Citrulline and the less common but industrially applicable D-Citrulline.
Ornithine is a basic amino acid with the chemical formula C5H12N2O2. It cannot be found in the proteins of living organisms and was discovered in 1877 by the scientist Jaffé in a hydrolysate of bird urine that had been fed benzoic acid, hence the name ornithine. It was later recognized as an important biological substance with many remarkable functions.
Tyrosine is a non-essential amino acid that plays a key role in a variety of biological processes, including neurotransmitter generation, protein synthesis and hormone regulation. As a precursor to key neurotransmitters such as norepinephrine, dopamine, and epinephrine, tyrosine has a significant effect on emotional, cognitive, and stress responses.
Serine plays a key role in many biological processes, being a building block of proteins and a precursor of various biomolecules. Characterized by its hydroxymethyl side chain, serine is not only integral to protein synthesis, but also participates in metabolic pathways, including the biosynthesis of other amino acids, nucleotides, and neurotransmitters.
Cysteine is a conditionally essential amino acid important for numerous biological functions because of its distinctive thiol (-SH) group, which enhances protein stability by forming disulfide bonds. It is also a precursor for glutathione, a crucial antioxidant that defends cells against oxidative stress.
Asparagine is a non-essential amino acid vital for protein synthesis and metabolism in both plants and animals. As one of the twenty standard amino acids, it enhances the structural and functional diversity of proteins by affecting their stability and activity. Beyond naturally occurring L-asparagine, numerous synthetic derivatives have been created to boost its applicability in research and industrial fields.
Aspartic acid is an important α-amino acid, which is mainly involved in various metabolic processes in the form of L-isomer. As a component of protein, aspartic acid plays a fundamental role in protein synthesis and promotes nitrogen metabolism through transamination.
Glutamine is one of the 20 natural amino acids. It is the most abundant amino acid in the blood and plays a key role in protein synthesis, cell energy production and immune system support. As an important component of various metabolic pathways, the biochemical significance of glutamine is that it can provide nitrogen for nucleotide biosynthesis and other nitrogen-containing compounds.
Proline is a unique amino acid with a distinctive cyclic structure, where the side chain forms a ring by bonding back to the amino group, creating a secondary amine. This ring structure imparts rigidity and limits hydrogen bonding, which is crucial for inducing turns in protein folding.
Lysine, an essential α-amino acid, is crucial for various biological functions. Characterized by its α-amino group, α-carboxylic acid group, and a side chain lysyl ((CH2)4NH2), lysine is a basic, charged amino acid at physiological pH.
Tryptophan is an essential amino acid found in various protein-containing foods and serves as a foundational element for several crucial biochemical pathways in the body. It is indispensable as humans cannot synthesize it autonomously, necessitating its intake through diet.
Phenylalanine is an essential amino acid that plays a crucial role in various physiological processes. Found naturally in many protein-rich foods and available as a dietary supplement, phenylalanine is vital for the production of neurotransmitters like dopamine, norepinephrine, and epinephrine.
Methionine is a crucial amino acid that plays a vital role in various biological processes, including protein synthesis, methylation, and antioxidant defense. While the natural forms of methionine, primarily L-methionine, are well-documented for their roles in health and nutrition, non-natural or synthetic methionine derivatives also offer significant benefits across multiple industries.
As an essential amino acid, leucine has a big impact on human health and a lot of industrial uses. It is a branched-chain amino acids (BCAAs) that is considered essential because the body is unable to synthesis it and has to get it from food. Its primary role lies in protein synthesis, where it serves as a key regulator of muscle growth and repair.
As one of the nine essential amino acids that the human body cannot synthesize, valine must be obtained through dietary sources, making its role indispensable in protein synthesis and overall health.
Histidine is an essential amino acid crucial for protein biosynthesis, immune response, and metal ion detoxification. It supports tissue growth, repair, and pH regulation, while also serving as a precursor to histamine, aiding in allergic reactions and inflammation.
Glycine is the simplest amino acid and plays a vital role in protein synthesis, especially in the production of collagen, and acts as an inhibitory neurotransmitter. Its benefits include supporting muscle growth, enhancing sleep quality, and boosting antioxidant defenses by aiding glutathione production
Alanine, an α-amino acid with the formula C₃H₇NO₂, is essential in protein synthesis and metabolic processes. As a non-essential amino acid, it is synthesized in the body from pyruvate and branched-chain amino acids.
Organic substances known as amino acids serve as the building blocks of proteins and are essential to many biological processes in living things. Amino acids are utilized in the pharmaceutical, food additive, animal feed, and cosmetics industries.
Amino acid analysis techniques include paper chromatography and thin layer chromatography, gas chromatography, high performance liquid chromatography, capillary electrophoresis, high performance anion exchange chromatography-integrated pulsed amperometric detection (HPAEC-IPA), etc.ric detection (HPAEC-IPA), etc.
As the building blocks of proteins and peptides, amino acids are essential for peptide synthesis and drug discovery due to their unique characteristics. Hydrophobic and hydrophilic amino acids are two significant classes of amino acids that possess distinct characteristics and can be applied in a variety of ways.
Amino acid is the basic unit of protein and plays an important role in the body's tissue composition. It is an important part of the body's survival, nutrition, metabolic regulation, immunity, and information transmission.
An amino acid is a compound with an amino group (-NH2) and a carboxyl group (-COOH) in the molecule. It has a common basic structure and contains complex functional groups, and is the basic unit of protein. Amino acids can be divided into α-, β-, γ-, ω-amino acids according to the different positions of the amino groups on the carbon chain, but the amino acids obtained after protein hydrolysis are all α-amino acids or imino acids.
Amino acids, peptides and proteins are important molecules that constitute living systems. Amino acids are the basic units of proteins, linked together by peptide bonds to form peptide chains, and multiple peptide chains make up proteins.
Aromatic amino acids (AAA) are a class of α-amino acids containing aromatic rings, including phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp). Among them, phenylalanine and tryptophan are essential amino acids.
Amino acids are the building blocks of proteins, the fundamental molecules that make up all living organisms. The order in which these amino acids are linked together forms the amino acid sequence, also known as the primary structure of a protein.
Amino acids are a class of amphoteric organic compounds containing alkaline amino groups and acidic carboxyl groups. They are the basic building blocks of biological functional macromolecule proteins.
Activity-based protein profiling (ABPP) technology has shown significant potential in the characterization of amino acid reactivity, which will aid in the discovery of new drug targets and the development of lead compounds.
The addition of non-canonical amino acids (ncAAs) offers a new possibility for site-specific conjugation. It requires the recombination of antibody sequences and the use of tRNAs and aminoacyl-tRNA synthetases (aaRSs) that are orthogonal to all endogenous tRNAs and synthetases in host cells to respond to unassigned codons for inserting ncAAs into proteins.
Bioorthogonal non-canonical amino acid tagging (BONCAT), based on intracellular introducing orthogonal chemoselective groups of small molecules, can realize specifically labeling, qualitative and quantitative analysis of newly translated proteins. etc.
Amino acids have been widely used in industrialized production, covering multiple industries such as food and health care, medicine, agriculture, and animal husbandry. In industry, amino acid synthesis methods are mainly divided into the following types: enzymatic method, extraction method, chemical synthesis method, fermentation method, etc.
Glucagon-like peptide-1 (GLP-1) receptor agonists are a class of drugs designed to mimic the actions of the natural peptide hormone GLP-1. GLP-1 is a gastrointestinal peptide released by L cells in the small intestine following nutrient ingestion.
The framework of non-ribosomal peptides (NRPs) is catalyzed by non-ribosomal peptide synthetases (NRPSs), and its assembly process includes loading of structural units, peptide chain elongation and modifications. NRPSs can hybridize with various biosynthetic pathways to form more complex structural types.
The production of orally active peptides requires a dual optimization process: 1) optimization of affinity and selectivity, and 2) optimization of oral efficacy. Chemical modifications of peptides have a significant impact on achieving the development of oral formulations.
Cell-targeting peptides are short peptides that specifically bind to receptors on the surface of specific types of cells and facilitate the targeted delivery of drug molecules, or other therapeutic molecules to these cells. These peptides are able to selectively recognize specific cells, thereby increasing the targeting of therapeutic molecules and the efficacy of drugs while reducing adverse effects on healthy cells.
According to their molecular structure, peptide synthetic reagents can be roughly divided into carbodiimides, phosphonium salts, uronium salts, organophosphorus, and other types of coupling reagents. Among them, carbodiimides, uronium salts, and phosphonium salts are the major three categories. Carbodiimides are first developed and most commonly used while uronium salts and phosphonium salts perform best with wide applications.
Peptide nucleic acid probes generally refer to short oligonucleotides of specific sequences consisting of 13-18 bases. Their base pairing is highly specific, allowing distinction between different nucleic acid sequences through single-base mismatches.
Peptide nucleic acid (PNA) is a synthetic analog of DNA with a peptide-like backbone. Introducing chiral functional groups at the γ-position in the PNA backbone allows for the formation of a right-handed helical structure, significantly enhancing its hybridization properties with target DNA/RNA.
Peptide nucleic acid (PNA) is a class of oligonucleotide analogs with a peptide backbone. Based on PNA's sequence specificity, it can selectively regulate the virus lifecycle at the genetic level, thereby effectively inhibiting the virus's survival and replication in host cells.
