TAILIEUCHUNG - Báo cáo khoa hoc : Membrane and surface interactions of Alzheimer’s Ab peptide – insights into the mechanism of cytotoxicity

Alzheimer’s disease is the most common form of dementia and its patho-logical hallmarks include the loss of neurones through cell death, as well as the accumulation of amyloid fibres in the form of extracellular neuritic pla-ques. | IFEBS Journal REVIEW ARTICLE Membrane and surface interactions of Alzheimer s Ab peptide - insights into the mechanism of cytotoxicity Thomas L. Williams and Louise C. Serpell Schoolof Life Sciences University of Sussex Falmer East Sussex UK Keywords Alzheimer s disease amyloid-b peptide calcein leakage GM1 ganglioside membrane bilayers protein misfolding Correspondence L. C. Serpell School of Life Sciences University of Sussex Falmer East Sussex BN1 9QG UK Fax 44 0 1273 678433 Tel 44 0 1273 877363 E-mail T. Williams Department of Physics Drexel University 12-908 3141 Chestnut Street Philadelphia PA 19104 USA Fax 1 215 895 5934 Tel 1 215 895 1989 E-mail tlw55@ Received 4 April 2011 revised 27 May 2011 accepted 20 June 2011 Alzheimer s disease is the most common form of dementia and its pathological hallmarks include the loss of neurones through cell death as well as the accumulation of amyloid fibres in the form of extracellular neuritic plaques. Amyloid fibrils are composed of the amyloid-b peptide Ab which is known to assemble to form toxic oligomers that may be central to disease pathology. Ab is produced by cleavage from the amyloid precursor protein within the transmembrane region and the cleaved peptide may retain some membrane affinity. It has been shown that Ab is capable of specifically binding to phospholipid membranes with a relatively high affinity and that modulation of the composition of the membrane can alter both membrane-amyloid interactions and toxicity. Various biomimetic membrane models have been used . lipid vesicles in solution and tethered lipid bilayers to examine the binding and interactions between Ab and the membrane surfaces as well as the resulting permeation. Oligomeric Ab has been observed to bind more avidly to membranes and cause greater permeation than fibrillar Ab. We review some of the recent advances in studying Ab-membrane interactions and discuss their implications with respect to .

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