tris(acetylacetonate)-aluminum(iii) and Neurodegenerative-Diseases

tris(acetylacetonate)-aluminum(iii) has been researched along with Neurodegenerative-Diseases* in 1 studies

Other Studies

1 other study(ies) available for tris(acetylacetonate)-aluminum(iii) and Neurodegenerative-Diseases

Article	Year
Potentiation of beta-folding of beta-amyloid peptide 25-35 by aluminum salts. Neuroscience letters, 1999, May-21, Volume: 267, Issue:1 The formation of the beta pleated configuration of the amyloid peptide fragment 25-35 in aqueous solution, has been studied using thioflavin-T fluorescence as an indicator of such folding. Both phosphate and adenosine triphosphate (ATP) enhance the formation of aggregated beta-sheets. This phosphate-induced aggregation is greater in the presence of aluminum sulfate in a dose dependent manner. In the absence of ATP or phosphate, aluminum salts do not promote aggregation. It is proposed that a particulate aluminum phosphate complex may form critical nuclei upon whose surface the amyloid peptide can change its configuration. This capacity for seeding may be a relevant factor in the formation of insoluble proteinaceous materials such as amyloid plaques and neurofibrillary tangles found in Alzheimer's disease. Topics: Alum Compounds; Amyloid beta-Peptides; Dose-Response Relationship, Drug; Drug Synergism; Humans; Neurodegenerative Diseases; Organometallic Compounds; Pentanones; Peptide Fragments; Protein Conformation; Protein Folding; Protein Structure, Secondary	1999

Article

Year

Potentiation of beta-folding of beta-amyloid peptide 25-35 by aluminum salts.

Neuroscience letters, 1999, May-21, Volume: 267, Issue:1

The formation of the beta pleated configuration of the amyloid peptide fragment 25-35 in aqueous solution, has been studied using thioflavin-T fluorescence as an indicator of such folding. Both phosphate and adenosine triphosphate (ATP) enhance the formation of aggregated beta-sheets. This phosphate-induced aggregation is greater in the presence of aluminum sulfate in a dose dependent manner. In the absence of ATP or phosphate, aluminum salts do not promote aggregation. It is proposed that a particulate aluminum phosphate complex may form critical nuclei upon whose surface the amyloid peptide can change its configuration. This capacity for seeding may be a relevant factor in the formation of insoluble proteinaceous materials such as amyloid plaques and neurofibrillary tangles found in Alzheimer's disease.

Topics: Alum Compounds; Amyloid beta-Peptides; Dose-Response Relationship, Drug; Drug Synergism; Humans; Neurodegenerative Diseases; Organometallic Compounds; Pentanones; Peptide Fragments; Protein Conformation; Protein Folding; Protein Structure, Secondary

1999