Control of Amyloid β‐Peptide Protofibril Formation by a Designed Template Assembly | Zendy

Dolphin Gunnar T. | Zendy; Dumy Pascal | Zendy; Garcia Julian | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

Control of Amyloid β‐Peptide Protofibril Formation by a Designed Template Assembly

Author(s) -

Dolphin Gunnar T.,

Dumy Pascal,

Garcia Julian

Publication year - 2006

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.200600395

Subject(s) - peptide , amyloid fibril , fibril , amyloid (mycology) , kinetics , computer science , chemistry , biophysics , nanotechnology , computational biology , biochemistry , crystallography , materials science , amyloid β , biology , medicine , physics , disease , inorganic chemistry , quantum mechanics

Insight into amyloids : Four identical segments of the amyloid β‐peptide, which is associated with Alzheimer's disease by fibril formation, were successfully attached to a cyclic decapeptide template. The assembly forms soluble protofibrils (see picture) that reveal a cross‐β‐sheet structure, with fast controllable kinetics and without a lag phase.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research