SCANNING-TUNNELING-MICROSCOPY STUDIES OF BETA-AMYLOID FIBRIL STRUCTURE AND ASSEMBLY

被引:16
作者
SHIVJI, AP
BROWN, F
DAVIES, MC
JENNINGS, KH
ROBERTS, CJ
TENDLER, SJB
WILKINSON, MJ
WILLIAMS, PM
机构
[1] UNIV NOTTINGHAM,DEPT PHARMACEUT SCI,BIOPHYS & SURFACE ANAL LAB,NOTTINGHAM NG7 2RD,ENGLAND
[2] SMITHKLINE BEECHAM PHARMACEUT,DEPT NEUROSCI,HARLOW CM19 5AD,ESSEX,ENGLAND
[3] SMITHKLINE BEECHAM PHARMACEUT,DEPT ANALYT SCI,BETCHWORTH RH3 7AJ,SURREY,ENGLAND
基金
英国工程与自然科学研究理事会;
关键词
ALZHEIMERS DISEASE; BETA-AMYLOID; AGGREGATION; SCANNING TUNNELING MICROSCOPY;
D O I
10.1016/0014-5793(95)00858-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Alzheimer's disease is in part characterised by the deposit of beta-amyloid peptide in the form of fibrils in the brain, In this study, the scanning tunnelling microscope (STM) has been used to provide high resolution images of synthetic fibril structure and formation as a function of time, Short fibrils are observed following brief peptide incubation times. At longer incubation periods ribbon like filaments were observed. These results suggest that beta-amyloid self-assembly is an ordered process, with a correlation between time of incubation and length of beta-amyloid filament growth.
引用
收藏
页码:25 / 28
页数:4
相关论文
共 31 条
[1]   GIANT MULTILEVEL CATION CHANNELS FORMED BY ALZHEIMER-DISEASE AMYLOID BETA-PROTEIN [A-BETA-P-(1-40)] IN BILAYER-MEMBRANES [J].
ARISPE, N ;
POLLARD, HB ;
ROJAS, E .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (22) :10573-10577
[2]   SURFACE STUDIES BY SCANNING TUNNELING MICROSCOPY [J].
BINNING, G ;
ROHRER, H ;
GERBER, C ;
WEIBEL, E .
PHYSICAL REVIEW LETTERS, 1982, 49 (01) :57-61
[3]  
BURDICK D, 1992, J BIOL CHEM, V267, P546
[4]   PROTEIN-PHOSPHORYLATION INHIBITS PRODUCTION OF ALZHEIMER AMYLOID-BETA/A4 PEPTIDE [J].
BUXBAUM, JD ;
KOO, EH ;
GREENGARD, P .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (19) :9195-9198
[5]   THE INFLUENCE OF AMINO-ACID-SEQUENCE ON THE FIBRILLOGENICITY AND AMYLOIDOGENICITY OF THE CARBOXY-TERMINUS OF BETA-AMYLOID PRECURSOR PROTEIN [J].
CAPUTO, CB ;
SOBEL, IRE ;
SYGOWSKI, LA ;
LAMPE, RA ;
SPREEN, RC .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1993, 306 (02) :321-330
[6]   ALZHEIMERS-DISEASE [J].
CHUN, MR ;
MAYEUX, R .
CURRENT OPINION IN NEUROLOGY, 1994, 7 (04) :299-304
[7]   PH-DEPENDENT STRUCTURAL TRANSITIONS OF ALZHEIMER AMYLOID PEPTIDES [J].
FRASER, PE ;
NGUYEN, JT ;
SUREWICZ, WK ;
KIRSCHNER, DA .
BIOPHYSICAL JOURNAL, 1991, 60 (05) :1190-1201
[8]   10 TO 14 RESIDUE PEPTIDES OF ALZHEIMERS-DISEASE PROTEIN ARE SUFFICIENT FOR AMYLOID FIBRIL FORMATION AND ITS CHARACTERISTIC X-RAY-DIFFRACTION PATTERN [J].
GOREVIC, PD ;
CASTANO, EM ;
SARMA, R ;
FRANGIONE, B .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1987, 147 (02) :854-862
[9]   SCANNING TUNNELING MICROSCOPY AND ATOMIC FORCE MICROSCOPY - APPLICATION TO BIOLOGY AND TECHNOLOGY [J].
HANSMA, PK ;
ELINGS, VB ;
MARTI, O ;
BRACKER, CE .
SCIENCE, 1988, 242 (4876) :209-216
[10]   AMYLOID DEPOSITION AS THE CENTRAL EVENT IN THE ETIOLOGY OF ALZHEIMERS-DISEASE [J].
HARDY, J ;
ALLSOP, D .
TRENDS IN PHARMACOLOGICAL SCIENCES, 1991, 12 (10) :383-388