|
Peptides
Peptides are short chains of amino acids linked by peptide bonds. A polypeptide is a longer, continuous, unbranched peptide chain. Polypeptides that have a molecular mass of 10,000 Dalton (unit), Da or more are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. Peptides fall under the broad chemical classes of biopolymer, biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others. Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligand (biochemistry), ligands such as coenzymes and cofactor (biochemistry), cofactors, to another protein or other macromolecule such as DNA or RNA, or to complex macromolecular assemblies. Amino acids that have been incorporated into peptides are termed Residue (chemistry)#Biochemistry, residues. A water molecule is released during formation of each amide bond.. Al ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Antimicrobial Peptides
Antimicrobial peptides (AMPs), also called host defence peptides (HDPs) are part of the innate immune response found among all classes of life. Fundamental differences exist between Prokaryote, prokaryotic and eukaryota, eukaryotic cells that may represent targets for antimicrobial peptides. These peptides are potent, broad spectrum antimicrobials which demonstrate potential as novel therapeutic agents. Antimicrobial peptides have been demonstrated to kill Gram negative and Gram positive bacteria, enveloped viruses, fungi and even transformed or cancerous cells. Unlike the majority of conventional antibiotics it appears that antimicrobial peptides frequently destabilize biological membranes, can form transmembrane channels, and may also have the ability to enhance immunity by functioning as immunomodulators. Structure Antimicrobial peptides are a unique and diverse group of molecules, which are divided into subgroups on the basis of their amino acid composition and structure. A ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cyclic Peptide
Cyclic peptides are polypeptide chains which contain a circular sequence of bonds. This can be through a connection between the amino and carboxyl ends of the peptide, for example in cyclosporin; a connection between the amino end and a side chain, for example in bacitracin; the carboxyl end and a side chain, for example in colistin; or two side chains or more complicated arrangements, for example in alpha-amanitin. Many cyclic peptides have been discovered in nature and many others have been synthesized in the laboratory. Their length ranges from just two amino acid residues to hundreds. In nature they are frequently antimicrobial or toxic; in medicine they have various applications, for example as antibiotics and immunosuppressive agents. Thin-layer chromatography, Thin-Layer Chromatography (TLC) is a convenient method to detect cyclic peptides in crude extract from bio-mass. Classification Cyclic peptides can be classified according to the types of bonds that comprise the ring ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. Only these 22 appear in the genetic code of life. Amino acids can be classified according to the locations of the core structural functional groups ( alpha- , beta- , gamma- amino acids, etc.); other categories relate to polarity, ionization, and side-chain group type ( aliphatic, acyclic, aromatic, polar, etc.). In the form of proteins, amino-acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling life on Earth and its emergence. Amino acids are formally named by the IUPAC- IUBMB Joint Commi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tetrapeptide
A tetrapeptide is a peptide, classified as an oligopeptide, since it only consists of four amino acids joined by peptide bonds. Many tetrapeptides are pharmacologically active, often showing affinity and specificity for a variety of receptors in protein-protein signaling. Present in nature are both linear and cyclic tetrapeptides (CTPs), the latter of which mimics protein reverse turns which are often present on the surface of proteins and druggable targets. Tetrapeptides may be cyclized by a fourth peptide bond or other covalent bonds. Examples of tetrapeptides are: * Tuftsin (L-threonyl-L-lysyl-L-prolyl-L-arginine) is a peptide related primarily to the immune system function. * Rigin (glycyl-L-glutaminyl-L-prolyl-L-arginine) is a tetrapeptide with functions similar to those of tuftsin. * Postin (Lys-Pro-Pro-Arg) is the N-terminal tetrapeptide of cystatin C and an antagonist of tuftsin. * Endomorphin-1 (H-Tyr-Pro-Trp-Phe-NH2) and endomorphin-2 (H-Tyr-Pro-Phe-Phe-NH2) a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptide Bond
In organic chemistry, a peptide bond is an amide type of covalent chemical bond linking two consecutive alpha-amino acids from C1 (carbon number one) of one alpha-amino acid and N2 (nitrogen number two) of another, along a peptide or protein chain. It can also be called a eupeptide bond to distinguish it from an isopeptide bond, which is another type of amide bond between two amino acids. Synthesis When two amino acids form a '' dipeptide'' through a ''peptide bond'', it is a type of condensation reaction. In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other. One loses a hydrogen and oxygen from its carboxyl group (COOH) and the other loses a hydrogen from its amino group (NH2). This reaction produces a molecule of water (H2O) and two amino acids joined by a peptide bond (−CO−NH−). The two joined amino acids are called a dipeptide. The ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metabolic reactions, DNA replication, Cell signaling, responding to stimuli, providing Cytoskeleton, structure to cells and Fibrous protein, organisms, and Intracellular transport, transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the Nucleic acid sequence, nucleotide sequence of their genes, and which usually results in protein folding into a specific Protein structure, 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called pep ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Opioid Peptide
Opioid peptides or opiate peptides are peptides that bind to opioid receptors in the brain; opiates and opioids mimic the effect of these peptides. Such peptides may be produced by the body itself, for example endorphins. The effects of these peptides vary, but they all resemble those of opiates. Brain opioid peptide systems are known to play an important role in motivation, emotion, attachment theory, attachment behaviour, the response to Stress (biology), stress and pain, Hunger (motivational state), control of food intake, and the rewarding effects of alcohol (drug), alcohol and nicotine. Opioid-like peptides may also be absorbed from partially digestion, digested food (casomorphins, Gluten exorphin, exorphins, and rubiscolins). opioid food peptides, Opioid peptides from food typically have lengths between 4–8 amino acids. Endogenous opioids are generally much longer. Opioid peptides are released by post-translational proteolytic cleavage of Protein precursor, precursor pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
N-terminus
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid, making it a chain. That leaves a free carboxylic group at one end of the peptide, called the C-terminus, and a free amine group on the other end called the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right (in LTR writing systems). This correlates the translation direction to the text direction, because when a protein is translated from messenger RNA, it is created from the N-terminus to the C-terminus, as amino acids are added to the carboxyl end of the protein. Chemistry Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Drosomycin
Drosomycin is an antifungal peptide from ''Drosophila melanogaster'' and was the first antifungal peptide isolated from insects. Drosomycin is induced by infection by the Toll signalling pathway, while expression in surface epithelia like the respiratory tract is instead controlled by the immune deficiency pathway (Imd). This means that drosomycin, alongside other antimicrobial peptides (AMPs) such as cecropins, diptericin, drosocin, metchnikowin and attacin, serves as a first line defence upon septic injury. However drosomycin is also expressed constitutively to a lesser extent in different tissues and throughout development. Structure Drosomycin is a 44-residue defensin-like peptide containing four disulfide bridges. These bridges stabilize a structure involving one α-helix and three β-sheets. Owing to these four disulfide bridges, drosomycin is resistant to degradation and the action of proteases. The cysteine stabilized αβ motif of drosomycin is also found in '' ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tripeptide
A tripeptide is a peptide derived from three amino acids joined by two or sometimes three peptide bonds. As for proteins, the function of peptides is determined by the constituent amino acids and their sequence. In terms of scientific investigations, the dominant tripeptide is glutathione (γ-L-Glutamyl-L-cysteinylglycine), which serves many roles in many forms of life. Examples * Eisenin (pGlu-Gln-Ala-OH) is a peptide with immunological activity that is isolated from the Japanese marine alga, ''Eisenia bicyclis'', which more commonly is known as Arame * GHK-Cu (glycyl-L-histidyl-L-lysine) is a human copper binding peptide with wound healing and skin remodeling activity, which is used in anti-aging cosmetics and more commonly referred to as copper peptide * Lactotripeptides (Ile-Pro-Pro and Val-Pro-Pro) found in milk products, act as ACE inhibitors * Leupeptin (''N''-acetyl-L-leucyl-L-leucyl-L-argininal) is a protease inhibitor that also acts as an inhibitor of calpain * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Dipeptide
A dipeptide is an organic compound derived from two amino acids. The constituent amino acids can be the same or different. When different, two isomers of the dipeptide are possible, depending on the sequence. Several dipeptides are physiologically important, and some are both physiologically and commercially significant. A well known dipeptide is aspartame, an artificial sweetener. Dipeptides are white solids. Many are far more water-soluble than the parent amino acids. For example, the dipeptide Ala-Gln has the solubility of 586 g/L more than 10x the solubility of Gln (35 g/L). Dipeptides also can exhibit different stabilities, e.g. with respect to hydrolysis. Gln does not withstand sterilization procedures, whereas this dipeptide does. Because dipeptides are prone to hydrolysis, the high solubility is exploited in infusions, i.e. to provide nutrition. Examples Commercial value About six dipeptides are of commercial interest. *Aspartame (''N''-L-α-aspartyl-L-phenylal ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Oligopeptide
An oligopeptide ('' oligo-'', "a few"), is a peptide consisting of two to twenty amino acids, including dipeptides, tripeptides, tetrapeptides, and other polypeptides. Some of the major classes of naturally occurring oligopeptides include aeruginosins, cyanopeptolins, microcystins, microviridins, microginins, anabaenopeptins, and cyclamides. Microcystins are best studied because of their potential toxicity impact in drinking water. A review of some oligopeptides found that the largest class are the cyanopeptolins (40.1%), followed by microcystins (13.4%). Production Oligopeptide classes are produced by nonribosomal peptides synthases (NRPS), except cyclamides and microviridins are synthesized through ribosomic pathways. Examples Examples of oligopeptides include: * Amanitins - Cyclic peptides taken from carpophores of several different mushroom species. They are potent inhibitors of RNA polymerases in most eukaryotic species, the prevent the production of mRNA and prote ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
