Amphotericin B interactions with soluble oligomers of amyloid Aβ1-42 peptide
| Autor: | Nicholas W. Smith, Onofrio Annunziata, Sergei V. Dzyuba |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Circular dichroism
Amyloid Clinical Biochemistry Pharmaceutical Science Peptide Biochemistry Oligomer chemistry.chemical_compound Biopolymers Amphotericin B Drug Discovery medicine Binding site Molecular Biology Protein secondary structure chemistry.chemical_classification Amyloid beta-Peptides Circular Dichroism Organic Chemistry P3 peptide Peptide Fragments Solubility chemistry Molecular Medicine medicine.drug |
| Zdroj: | Bioorganic & Medicinal Chemistry. 17:2366-2370 |
| ISSN: | 0968-0896 |
| Popis: | Amphotericin B has recently been suggested as an efficient inhibitor of amyloid peptide fibril formation; however its interactions with more neurotoxic, soluble forms of amyloid peptides have not been reported to date. Circular dichroism spectroscopy allowed for distinguishing between the binding and inhibition of aggregation events: amphotericin B distinctly interacts with both unordered and ordered, beta-structure-rich soluble oligomeric forms of Abeta1-42 peptide, yet amphotericin B has no measurable impact neither on the secondary structure nor on time-dependent aggregation profile of the amyloid peptide. |
| Databáze: | OpenAIRE |
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