Probing The Mechanism Of Insulin Aggregation With Added Metalloporphyrins
Document Type
Article
Publication Date
3-4-2008
Published In
Biochemistry
Abstract
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.
Recommended Citation
S. P. Sibley, K. Sosinsky, L. E. Gulian, E. J. Gibbs, and Robert F. Pasternack.
(2008).
"Probing The Mechanism Of Insulin Aggregation With Added Metalloporphyrins".
Biochemistry.
Volume 47,
Issue 9.
2858-2865.
DOI: 10.1021/bi701682r
https://works.swarthmore.edu/fac-chemistry/145