Role for the alpha-Helix in Aberrant Protein Aggregation

RANI KUNJITHAPATHAM; FABIANA Y. OLIVA; URMI DOSHI; MAR PÉREZ; JESUS Á VILA; VICTOR MUÑOZ

BIOCHEMISTRY

American Chemical Society

Lugar: USA; Año: 2005 vol. 44 p. 149 - 149

0006-2960

font face="Times New Roman" size="3"> Is the alpha-helix structure capable of triggering the formation of aberrant protein aggregates? To answer this question, we investigate the in Vitro aggregation of tau protein in the presence of the helix inducing agent TFE. Tau is a natively unfolded protein that binds to microtubules and forms aggregates in Alzheimer?s disease. We find that full-length tau has residual alpha-helix structure, which is further enhanced by three mutations involved in genetic neurological disorders. TFE concentrations matching an alpha