Experimental inhibition of peptide fibrillogenesis by synthetic peptides, carbohydrates and drugs.

作者: Alagiri Srinivasan

DOI: 10.1007/978-94-007-5416-4_12

关键词: Small moleculeFibril formationAmyloidBiophysicsFibrilPeptideChemistryFibrillogenesisCongo redIn vitro

摘要: Peptide fibrillogenesis generally begins by the transformation of normally soluble proteins into elongated aggregates which are called as amyloid. These fibrils mainly consist s-sheets. They share certain common characteristics such a cross-s x-ray diffraction pattern, association with other and typical staining dye Congo Red. The individual form deposit consists disease-specific peptide/protein. protein serves basis for classification amyloids. fibril-forming peptides/proteins diseases makes them primary disease-targets. Understanding molecular interactions involved in fibril formation becomes foremost requirement to characterize target. Interference these s-sheets vitro prevents sometimes reverses assembly. A small molecule capable interfering could have therapeutic applications diseases. This anti-aggregation approach appears be viable treatment option. search is pursued actively world over. All types compounds approaches slow down or prevent aggregation process been described literature. efforts reviewed this chapter.

参考文章(144)
J. Robin Harris, Nathaniel G.N. Milton, Cholesterol in Alzheimer's disease and other amyloidogenic disorders. Sub-cellular biochemistry. ,vol. 51, pp. 47- 75 ,(2010) , 10.1007/978-90-481-8622-8_2
N.M. Green, N.G. Wrigley, W.C. Russell, S.R. Martin, A.D. McLachlan, Evidence for a repeating cross-beta sheet structure in the adenovirus fibre. The EMBO Journal. ,vol. 2, pp. 1357- 1365 ,(1983) , 10.1002/J.1460-2075.1983.TB01592.X
Alexander Kurz, Robert Perneczky, Amyloid clearance as a treatment target against Alzheimer's disease. Journal of Alzheimer's Disease. ,vol. 24, pp. 61- 73 ,(2011) , 10.3233/JAD-2011-102139
Jian-Ping Guo, Sheng Yu, Patrick L. McGeer, Simple In Vitro Assays to Identify Amyloid-β Aggregation Blockers for Alzheimer's Disease Therapy Journal of Alzheimer's Disease. ,vol. 19, pp. 1359- 1370 ,(2010) , 10.3233/JAD-2010-1331
N. Ferguson, J. Becker, H. Tidow, S. Tremmel, T. D. Sharpe, G. Krause, J. Flinders, M. Petrovich, J. Berriman, H. Oschkinat, A. R. Fersht, General structural motifs of amyloid protofilaments Proceedings of the National Academy of Sciences of the United States of America. ,vol. 103, pp. 16248- 16253 ,(2006) , 10.1073/PNAS.0607815103
Justin J Yerbury, Stephen Poon, Sarah Meehan, Brianna Thompson, Janet R. Kumita, Christopher M. Dobson, Mark R. Wilson, The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures The FASEB Journal. ,vol. 21, pp. 2312- 2322 ,(2007) , 10.1096/FJ.06-7986COM
Gianluigi Forloni, Laura Colombo, Laura Girola, Fabrizio Tagliavini, Mario Salmona, Anti‐amyloidogenic activity of tetracyclines: studies in vitro FEBS Letters. ,vol. 487, pp. 404- 407 ,(2001) , 10.1016/S0014-5793(00)02380-2
Jean-Christophe Rochet, Peter T Lansbury, Amyloid fibrillogenesis: themes and variations. Current Opinion in Structural Biology. ,vol. 10, pp. 60- 68 ,(2000) , 10.1016/S0959-440X(99)00049-4
X. Hu, S. L. Crick, G. Bu, C. Frieden, R. V. Pappu, J.-M. Lee, Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide Proceedings of the National Academy of Sciences of the United States of America. ,vol. 106, pp. 20324- 20329 ,(2009) , 10.1073/PNAS.0911281106