Use of surface plasmon resonance to study the elongation kinetics and the binding properties of the highly amyloidogenic Aβ(1-42) peptide, synthesized by depsi-peptide technique.

@article{Stravalaci2011UseOS,
  title={Use of surface plasmon resonance to study the elongation kinetics and the binding properties of the highly amyloidogenic Aβ(1-42) peptide, synthesized by depsi-peptide technique.},
  author={Matteo Stravalaci and Marten Beeg and Mario Salmona and Marco Gobbi},
  journal={Biosensors & bioelectronics},
  year={2011},
  volume={26 5},
  pages={2772-5}
}
A wide variety of human diseases are associated with the formation of highly organized protein aggregates termed amyloid fibrils, whose growth (elongation) is due to the assembly of the basic molecular units (monomers) in a sequential polymerization process. Surface plasmon resonance (SPR) technology has been proposed as a powerful approach to study in detail the fibril elongation of some amyloidogenic peptides. In particular, the injection of monomers over immobilized fibrils allows to follow… CONTINUE READING

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