Protein Aggregation and Self-Assembly Analysis by AFM and FTIR Microscopy

 

Thursday, March 8, 2012

USA 11:00 a.m. EST / 10:00 a.m. CST / 8:00 a.m. PST / 16:00 GMT

 

Self-assembly and aggregation of proteins and peptides are critical elements of biochemical processes in nature. Misfolded proteins and incorrect protein assembly have been implicated in diseases such as Type 2 diabetes and Alzheimer's disease. This talk will cover AFM analysis of self-assembly of two different systems, hydrophobin proteins isolated from Agaricus bisporus (white button mushroom) responsible for regulating interfacial processes in fungi, and Amyloid-b (Ab) peptides known to be involved in Alzheimer's disease. Both systems display nanoscale fibrillar structures under specific environmental conditions, and assembly can be disrupted by changes in the environment. AFM allows visualization and greater understanding of the processes involved in self-assembly.

FTIR spectroscopy and FTIR microscopy can be used for identifying biological samples separated by only a few microns, real-time monitoring of fast dynamical behavior, and characterizing the chemical structure with high spatial resolution over large biologically relevant areas. In this talk, infrared microspectroscopy utilizing a focal plane array will be discussed. The FT-IR analyses of several biological samples (including the chemical imaging of the Hippocampus section from mice to study Alzheimer's disease) will be reviewed.