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Motilin is a 22-amino acid polypeptide hormone in the motilin family that, in humans, is encoded by the MLN gene. [2]Motilin is secreted by endocrine Mo cells [3] [4] (also referred to as M cells, which are not the same as the M cells, or microfold cells, found in Peyer's patches) that are numerous in crypts of the small intestine, especially in the duodenum and jejunum. [5]
Insulin-treated athletes are perceived to have lean body mass because physiological hyperinsulinemia in human skeletal muscle improves the activity of amino acid transport, which in turn promotes protein synthesis. [78] Insulin stimulates the transport of amino acids into cells and also controls glucose metabolism.
Plecanatide is a 16 amino acid peptide with the amino acid sequence: H-Asn 1-Asp 2-Glu 3-Cys 4-Glu 5-Leu 6-Cys 7-Val 8-Asn 9-Val 10-Ala 11-Cys 12-Thr 13-Gly 14-Cys 15-Leu 16-OH (one-letter sequence: NDECELCVNVACTGCL). Plecanatide is nearly structurally identical to human uroguanylin, apart from the substitution of Asp 3 with Glu 3. [13]
Insulin degludec is a modified insulin that has one single amino acid deleted in comparison to human insulin, and is conjugated to hexadecanedioic acid via gamma-L-glutamyl spacer at the amino acid lysine at position B29. It is included on the World Health Organization's List of Essential Medicines [11] as an equivalent to insulin glargine.
The amino acid sequence of animal insulins in different mammals may be similar to human insulin (insulin human INN), there is however considerable viability within vertebrate species. [16] Porcine insulin has only a single amino acid variation from the human variety, and bovine insulin varies by three amino acids.
Insulin glulisine, sold under the brand name Apidra among others, is a rapid-acting modified form of medical insulin used for the treatment of diabetes.It differs from human insulin in that the amino acid asparagine at position B3 is replaced by lysine and the lysine in position B29 is replaced by glutamic acid. [2]
Exenatide binds to the intact human Glucagon-like peptide-1 receptor (GLP-1R) in a similar way to the human peptide glucagon-like peptide-1 (GLP-1); exenatide bears a 50% amino acid homology to GLP-1 and it has a longer half-life in vivo. [22] Exenatide is believed to facilitate glucose control in at least five ways:
The connection between the A chain and C peptide is much more stable than the junction between the C peptide and B chain, with alpha helical features being exhibited near the C peptide-A chain connection. [10] The C peptide-A chain junction occurs between residues 64 and 65 of proinsulin. These are lysine and arginine molecules, respectively. [10]