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α-Amanitin Bacitracin Ciclosporin. Cyclic peptides are polypeptide chains which contain a circular sequence of bonds. [1] 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 ...
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. [1]
During the course of the docking process, the ligand and the protein adjust their conformation to achieve an overall "best-fit" and this kind of conformational adjustment resulting in the overall binding is referred to as "induced-fit". [5] Molecular docking research focuses on computationally simulating the molecular recognition process.
The active ingredient was later determined to be a cyclic peptide, named kalata B1, after the traditional name for the tea, kalata-kalata. Although in vivo studies in rats confirmed the uterotonic activity of the purified peptide, it was another 20 years before the cyclic cystine knot motif and structure of the purified peptide were elucidated ...
α-Amanitin (alpha-Amanitin) is a cyclic peptide of eight amino acids.It is possibly the most deadly of all the amatoxins, toxins found in several species of the mushroom genus Amanita, one being the death cap (Amanita phalloides) as well as the destroying angel, a complex of similar species, principally 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 death domain (DD) is a protein interaction module composed of a bundle of six alpha-helices. DD is a subclass of protein motif known as the death fold and is related in sequence and structure to the death effector domain and the caspase recruitment domain , which work in similar pathways and show similar interaction properties. [2]
DKP's are the smallest known class of cyclic peptide. [1] Despite their name, they are not ketones, but amides. Three regioisomers are possible, differing in the locations of the carbonyl groups. Retosiban [2] is a diketopiperazine being investigated as an oral drug. One isomer is an oxamide obtained from ethylenediamine.