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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.
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.
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.
