Explore chapters and articles related to this topic
Arsenals of Pharmacotherapeutically Active Proteins and Peptides: Old Wine in a New Bottle
Published in Debarshi Kar Mahapatra, Swati Gokul Talele, Tatiana G. Volova, A. K. Haghi, Biologically Active Natural Products, 2020
On the basis of number of amino acids present, peptides can be classified as: Dipeptide which contains two amino acid residues.Tripeptide which contains three amino acid residues.Tetrapeptide which contains four amino acid residues.Oligopeptides which contain less than 10 amino acid residues.Polypeptides which contain 50 or less than 50 amino acid residues.
Nanostructured Cellular Biomolecules and Their Transformation in Context of Bionanotechnology
Published in Anil Kumar Anal, Bionanotechnology, 2018
Amino acids are linked together in a polypeptide chain by peptide bond. The linkage between amino acids occurs through simple condensation reaction between the α-amino groups of one amino acid with α-carboxyl group of another amino acid with the release of a water molecule. Linked amino acids in a polypeptide chain are called amino acid residues. The free amino group and carboxyl group at the opposite ends of peptide chain are called the N-terminal and C-terminal, respectively. During protein synthesis, polypeptide chain formation starts from N-terminal of amino acid (usually methionine) and continues toward the C-terminals by adding one amino acid at a time. Depending on the number of amino acids linked together, they are termed as dipeptide, tripeptide, oligopeptide, and polypeptide. Dipeptide contains two amino acids linked by one peptide bond. Therefore, each peptide chain has one free amino and carboxyl group at opposite ends (Moran et al. 2012).
Amino Acids, Peptides, and Proteins
Published in Michael B. Smith, A Q&A Approach to Organic Chemistry, 2020
A dipeptide is a molecule composed of two amino acid residues. A pentapeptide is a molecule composed of five amino acid residues. What is a residue?
Insight into intermolecular interactions and hydration properties of biologically active amino acids in aqueous solutions of cefepime: volumetric, compressibility and viscometric studies
Published in Journal of Dispersion Science and Technology, 2021
Suvarcha Chauhan, Neetika Kumari, Lalita Pathania
The drug − protein interactions are generally difficult to study because of the complex structure of protein molecules. However, to reduce the degree of complexity, it is useful to investigate the solution behavior of model compounds such as amino acids, dipeptides etc. Drug can interact with these amino acids and small peptides to change the conformation of proteins either by stabilizing or destabilizing them. The recognition of drug-amino acid/peptide interactions in aqueous solution has always been a matter of interest.[3,4] Therefore, physico-chemical investigations are carried out for amino acids/peptides in aqueous solutions of different types of drugs. Among amino acids and peptides, glycine and glycylglycine have been chosen for the present study. Glycine is the simplest possible amino acid and is biosynthesized in the body from the amino acid serine.[5] It plays an important role in the body's production of DNA, phospholipids and collagen, and in release of energy besides acting as neurotransmitter. Glycylglycine is dipeptide made up of two glycine molecules joined by peptide linkage and is used in the synthesis of more complicated peptides.
Theoretical study of the mechanism of 2,5-diketopiperazine formation during pyrolysis of proline
Published in Molecular Physics, 2020
Cristian Cervantes, José R. Mora, Luis Rincón, Vladimir Rodríguez
Scheme 1 shows the proposed mechanism for pyrolysis of proline. This mechanism is based on the suggestion of Chiavari et al [8], who mentioned that ‘the thermal decomposition involves a double dehydration reaction yielding firstly the dipeptide and subsequently the 2,5-diketopiperazine’. In this work, it is proposed that the dipeptide is formed after two elementary steps: two molecules of proline (2R) are bonded by a condensation reaction producing a dimer with a diol group (INT1), which then transfers a proton that forms a molecule of water, initiates the first dehydration, and produces the dipeptide (INT2). After that, another two elementary steps are proposed: a cyclisation process based on the intramolecular reaction between the amine and carboxyl groups generating a cycle with another diol group (INT3), which also transfers a proton producing the second dehydration and finally obtaining the 2,5-diketopiperazine product (P).
Carnosine in health and disease
Published in European Journal of Sport Science, 2019
Guilherme Giannini Artioli, Craig Sale, Rebecca Louise Jones
Carnosine and its analogues (anserine and balenine) are naturally-occurring histidine-containing dipeptides (HCDs) expressed in different tissues, such as skeletal muscle, cardiac muscle, kidneys, and some regions of the brain. Roles of HCDs include: neutralisation of reactive species, detoxification and acid-base regulation.