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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Liu, Kuan-nan Han, Tzu-chiang Wang, Steven S-s |
| Description | Author Affiliation: Wang SS ( Department of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan. sswang@ntu.edu.tw) |
| Abstract | Amyloid fibrils have been associated with at least 25 different degenerative diseases. The 51-residue polypeptide hormone insulin, which is associated with type II diabetes, has been shown to self-assemble to form amyloid fibrils in vitro . With bovine insulin as a model, the research presented here explores the effects of two amphiphilic surfactants (1,2-dihexanoyl-sn-glycero-3-phosphocholine (di-C7-PC) and 1,2-diheptanoyl-sn-glycero-3-phosphocholine (di-C7-PC)) on the in vitro fibrillation process of bovine insulin at pH 2.0 and 55 °C. We demonstrated that insulin fibrillation may be inhibited by both surfactants in a dose-dependent fashion. The best inhibition of fibril formation is observed when insulin is incubated with 4 mM di-C7-PC. Moreover, the addition of either surfactant at the concentrations studied attenuated insulin fibril-induced cytotoxicity in both PC12 and SH-SY5Y cell lines. The results from this work may contribute to the understanding of the molecular factors affecting amyloid fibrillation and the molecular mechanism(s) of the interactions between the membrane and amyloid proteins. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 6 |
| Volume Number | 1802 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2010-06-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Amyloid Biosynthesis Insulin Metabolism Toxicity Surface-Active Agents Pharmacology Chemistry Ultrastructure Amyloidosis Drug Therapy Animals Cell Line Cell Survival Drug Effects In Vitro Techniques Microscopy, Electron, Transmission Models, Biological PC12 Cells Phosphatidylcholines Phospholipid Ethers Protein Multimerization Protein Structure, Secondary Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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