Amylin (human) trifluoroacetate salt
Amylin (human) trifluoroacetate salt structure
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Common Name | Amylin (human) trifluoroacetate salt | ||
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| CAS Number | 122384-88-7 | Molecular Weight | 3903.28000 | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C165H261N51O55S2 | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells.
Proc. Natl. Acad. Sci. U. S. A. 84 , 3881, (1987) Amyloid deposits localized to the islets of Langerhans are typical of non-insulin-dependent human diabetes mellitus and of diabetes mellitus in adult cats. Amyloid deposits also commonly occur in insulin-producing pancreatic tumors. We have purified a major p... |
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Structure and thermodynamics of amylin dimer studied by Hamiltonian-temperature replica exchange molecular dynamics simulations. Laghaei R, Mousseau N, Wei G.
J. Phys. Chem. B 115 , 33146-3154, (2011)
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Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.
Proc. Natl. Acad. Sci. U. S. A. 84 , 8628, (1987) Deposition of amyloid in pancreatic islets is a common feature in human type 2 diabetic subjects but because of its insolubility and low tissue concentrations, the structure of its monomer has not been determined. We describe a peptide, of calculated molecula... |
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Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology.
Biochim. Biophys. Acta 1537 , 179-203, (2001) Islet amyloid polypeptide (IAPP, amylin) is secreted from pancreatic islet beta-cells and converted to amyloid deposits in type 2 diabetes. Conversion from soluble monomer, IAPP 1-37, to beta-sheet fibrils involves changes in the molecular conformation, cellu... |
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Islet amyloid: a complication of islet dysfunction or an aetiological factor in Type 2 diabetes?
Diabetologia 47 , 157-169, (2004) The role of islet amyloidosis in the onset and progression of Type 2 diabetes remains obscure. Islet amyloid polypeptide is a 37 amino-acid, beta-cell peptide which is co-stored and co-released with insulin. Human islet amyloid polypeptide refolds to a beta-c... |
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Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment.
Biochim. Biophys. Acta 1808 , 2337-2342, (2011) Human islet amyloid polypeptide is a hormone coexpressed with insulin by pancreatic beta-cells. For reasons not clearly understood, hIAPP aggregates in type II diabetics to form oligomers that interfere with beta-cell function, eventually leading to the loss ... |
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Stable and metastable states of human amylin in solution.
Biophys. J. 99 , 2208-2216, (2010) Patients with type II diabetes exhibit fibrillar deposits of human amylin protein in the pancreas. It has been proposed that amylin oligomers arising along the aggregation or fibril-formation pathways are important in the genesis of the disease. In a step tow... |
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Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy.
Biochemistry 47 , 12689-12697, (2008) Disruption of the cellular membrane by the amyloidogenic peptide IAPP (or amylin) has been implicated in beta-cell death during type 2 diabetes. While the structure of the mostly inert fibrillar form of IAPP has been investigated, the structural details of th... |