Elucidating the Kinetics of β-amyloid Fibril Formation
| dc.contributor.author | Edwin, Nadia J. | |
| dc.date.accessioned | 2021-10-10T14:37:15Z | |
| dc.date.available | 2021-10-10T14:37:15Z | |
| dc.date.issued | 2005 | |
| dc.description.abstract | The formation of β-Amyloid peptide (Aβ1-40) aggregates was monitored by dynamic light scattering. Various sizes of materials may be present throughout the aggregation process, but small scatterers are difficult to detect in the presence of large ones. Fluorescence photobleaching recovery studies on 5-carboxyfluorescein-labeled Aβ1-40 peptide solutions readily confirmed the presence of large and small species simultaneously. The effects of dye substitution on the aggregation behavior of Aβ1-40 peptide are subtle, but should not prevent further investigations by fluorescence photobleaching recovery or other fluorescence methods. | en_US |
| dc.identifier.citation | Edwin, N. J., Bantchev, G. B., Russo, P. S., Hammer, R. P., & McCarley, R. L. (2005). Elucidating the kinetics of β-amyloid fibril formation. In L. S. Korugic-Karasz, W. J. MacKnight, & E. Martuscelli (Eds.), New polymeric materials (pp. 106-118). American Chemical Society. https://doi.org/10.1021/bk-2005-0916.ch009 | en_US |
| dc.identifier.uri | https://doi.org/10.1021/bk-2005-0916.ch009 | |
| dc.identifier.uri | http://hdl.handle.net/20.500.12521/193 | |
| dc.language.iso | en | en_US |
| dc.publisher | American Chemical Society | en_US |
| dc.title | Elucidating the Kinetics of β-amyloid Fibril Formation | en_US |
| dc.type | Book chapter | en_US |