| Autor: |
Sibley SP; Department of Chemistry, Goucher College, Baltimore, Maryland 21204, USA. ssibley@goucher.edu, Sosinsky K, Gulian LE, Gibbs EJ, Pasternack RF |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemistry [Biochemistry] 2008 Mar 04; Vol. 47 (9), pp. 2858-65. Date of Electronic Publication: 2008 Jan 26. |
| DOI: |
10.1021/bi701682r |
| Abstrakt: |
The mechanism of inhibition of insulin-based amyloid gel formation by metal derivatives of tetrakis(4-sulfonatophenyl)porphyrin has been investigated. Time-course UV/vis measurements in conjunction with atomic force microscopy (AFM) were used to study the correlation between observed kinetics and amyloid structure for various concentration ranges of added metalloporphyrins. Observed structures include fibrils as well as circular, ring-like structures formed as a result of the interaction of insulin with porphyrin. In addition, binding studies demonstrate that the effectiveness of inhibition of the various metalloporphyrins is directly related to the strength of binding to insulin. It is suggested that both the electron distribution in the porphyrin core and the tendency to form porphyrin dimers affect both the structure of amyloid formed and the kinetic profile of the reaction. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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