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Canine epileptoid cramping syndrome (CECS), previously known as Spike's disease, is a hereditary dog disease initially found in Border Terriers and has since been documented in many other dog breeds including Labrador Retrievers and Chihuahuas, with similarities to canine epilepsy.
Crystal structure of an extracellular segment of integrin alphaVbeta3 complexed with a cyclic peptide containing the arginyl-glycyl-aspartic acid (RGD) sequence. RGD is shown in maroon. CEND-1, also known as iRGD , is a cyclic peptide that homes to tumors via binding to integrin alpha V receptors. [ 22 ]
Once a cyclic peptide is identified with a biological activity of interest, it may also be possible to identify the target of the peptide (a gene that encodes a protein with which it interacts) by functional complementation, facilitating a better understanding of its mechanism of action.
The phallotoxins consist of at least seven compounds, all of which are bicyclic heptapeptides (seven amino acids), isolated from the death cap mushroom (Amanita phalloides). They differ from the closely related amatoxins by being one residue smaller, both in the final product and the precursor protein.
Amatoxin is the collective name of a subgroup of at least nine related cyclic peptide toxins found in three genera of deadly poisonous mushrooms (Amanita, Galerina and Lepiota) and one species of the genus Pholiotina. [1] Amatoxins are very potent, as little as half a mushroom cap can cause severe liver injury if swallowed.
β-Amanitin (beta-Amanitin) is a cyclic peptide comprising eight amino acids. It is part of a group of toxins called amatoxins, which can be found in several mushrooms belonging to the genus Amanita. Some examples are the death cap (Amanita phalloides) and members of the destroying angel complex, which includes A. virosa and A. bisporigera.
Phalloidin was one of the first cyclic peptides to be discovered. It was isolated from the death cap mushroom and crystallized by Feodor Lynen and Ulrich Wieland [1] in 1937. [2] Its structure is unusual in that it contains a cysteine-tryptophan linkage to form a bicyclic heptapeptide. This linkage had not been characterized before and makes ...
The cyclic peptide NR58-3.14.3 was shown to be a powerful anti-inflammatory agent in vivo inhibiting inflammation in a number of disease models such as atherosclerosis, [4] ischemia, [5] [6] [7] lung disease, [8] surgical adhesions, [9] endometriosis [10] and pulmonary graft-versus-host disease. [11]