Title : In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: new insights into mechanism of beta-sheet formation.

Pub. Date : 1999 Mar 30

PMID : 10097098






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 We have applied in situ atomic force microscopy to directly observe the aggregation of Alzheimer"s beta-amyloid peptide (Abeta) in contact with two model solid surfaces: hydrophilic mica and hydrophobic graphite. Graphite amyloid beta precursor protein Homo sapiens
2 We have applied in situ atomic force microscopy to directly observe the aggregation of Alzheimer"s beta-amyloid peptide (Abeta) in contact with two model solid surfaces: hydrophilic mica and hydrophobic graphite. Graphite amyloid beta precursor protein Homo sapiens
3 In contrast, on hydrophobic graphite Abeta formed uniform, elongated sheets. Graphite amyloid beta precursor protein Homo sapiens
4 The sheets of Abeta were oriented along three directions at 120 degrees to each other, resembling the crystallographic symmetry of a graphite surface. Graphite amyloid beta precursor protein Homo sapiens