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Of amino acids on insulin fiber formation and cell toxicity
PAGE \* MERGEFORMAT 6
Of amino acids on insulin fiber formation and cell toxicity
Author: Wang Min, ZHANG Xian-qing, HE Jing, Zeng Cheng Ming
[Abstract] Objective: To study the amino acids of the bovine insulin amyloid fibrils formation, morphology and cell toxicity. Methods: Sulfur hormone (ThT) fluorescence detection of bovine insulin to form amyloid fibers kinetic curve, transmission electron microscopy observation of fiber morphology; to amyloid fibrils induced aggregation of human red blood cells and hemolytic for the indicators to assess the role of fiber cell membrane damage. Results: bovine insulin at pH 1.6,57 ℃ under the conditions of 1.5 h began to form in amyloid fibers, five kinds of amino acids that the group of histidine (His), proline (Pro), threonine (Thr), glutamine (Gln) and arginine (Arg) with a delayed insulin fibrosis, has also changed the form of amyloid fibers. insulin in the formation of amyloid fibers after a lower concentration range and aggregation induced by human red blood cell hemolysis, the role of the gradual increase along with the growth of fibers. Although the amino acid delayed the growth of the fiber under the action of the fibers with different patterns, but it does not changes in cell membrane damage of fiber. Conclusion: bovine insulin in the formation of amyloid fibrils after the destructive role of cell membrane structure. amino acids can inhibit insulin fibrosis. Insulin-fiber effect of red cell membrane damage has nothing to do with their morphology and growth kinetics.
[Keywords:] amyloid fibers; bovine insulin; amino acids; red blood cell; amyloidosis
0 Introduction
Under certain conditions, many proteins due to misfolding and the formation of amyloid fibrils deposition, has been found that at least 20 kinds of human diseases and due to protein misfolding caused by the deposition of amyloid fibrils [1-4]. Insulin-like protein under certain conditions, easy to form amyloid fibrils which may lead to the pati
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