Title : Promotion of beta-structure by interaction of diabetes associated polypeptide (amylin) with phosphatidylcholine.

Pub. Date : 1992 Aug 21

PMID : 1504094






5 Functional Relationships(s)
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1 Promotion of beta-structure by interaction of diabetes associated polypeptide (amylin) with phosphatidylcholine. Phosphatidylcholines islet amyloid polypeptide Homo sapiens
2 The interaction of the diabetes associated polypeptide (amylin) with dimyristoylphosphatidylcholine (DMPC) was assessed by measurements of turbidity (absorbance at 400 nm) and secondary structure by CD spectroscopy. Dimyristoylphosphatidylcholine islet amyloid polypeptide Homo sapiens
3 The interaction of the diabetes associated polypeptide (amylin) with dimyristoylphosphatidylcholine (DMPC) was assessed by measurements of turbidity (absorbance at 400 nm) and secondary structure by CD spectroscopy. Dimyristoylphosphatidylcholine islet amyloid polypeptide Homo sapiens
4 In trifluoroethanol, human amylin adopts a highly alpha-helical conformation while the rat peptide is less structured. Trifluoroethanol islet amyloid polypeptide Homo sapiens
5 These data demonstrate that fundamental differences in the structures adopted by amylins from human and rat species exist in mixtures with DMPC and suggest that these differences may be related to the formation of amyloid fibrils in the human amylin peptide which are not observed in the rat peptide. Dimyristoylphosphatidylcholine islet amyloid polypeptide Homo sapiens