What is it about?
Aβ(12-28) formed antiparallel β sheets within minutes after lowering the pH by photolytic release of protons from caged sulfate. This was observed for end-protected and non-protected peptides indicating that charges at the peptide ends do not influence the architecture of the β sheets .
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Why is it important?
Alzheimer's disease is one of the main neurodegenerative diseases. Our work shows that initial aggregates form very fast at low pH.
Perspectives
Please note that we published a correction of this work (J. Phys. Chem. B, 2014, 118 (11), pp 3243–3244, DOI: 10.1021/jp5010242). Only one type of aggregates was detected.
Professor Andreas Barth
Stockholm University
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This page is a summary of: Formation of Two Different Types of Oligomers in the Early Phase of pH-Induced Aggregation of the Alzheimer Aβ(12-28) Peptide, The Journal of Physical Chemistry B, October 2012, American Chemical Society (ACS),
DOI: 10.1021/jp305015g.
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