Amyloid protein (Ab1–40) aggregation and conformation was examined using native and sodium dodecyl sulfate/ polyacrylamide gel electrophoresis,and the results com-pared with those obtained by atomic force microscopy, and with Congo red binding,sedimentation and turbidity assays. The amount of Ab aggregation measured was different,depending upon the method used. Incubation for 15 min at pH or in the presence of Fe 2+ ,Cu 2+ or Zn 2+ did not alter the level of Aboligomers observed on SDS and native gels
