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Natural tri- to hexapeptides self-assemble in water to amyloid β-type fiber aggregates by unexpected...

Natural tri- to hexapeptides self-assemble in water to amyloid β-type fiber aggregates by unexpected...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmed_primary_21205900

Natural tri- to hexapeptides self-assemble in water to amyloid β-type fiber aggregates by unexpected α-helical intermediate structures

About this item

Full title

Natural tri- to hexapeptides self-assemble in water to amyloid β-type fiber aggregates by unexpected α-helical intermediate structures

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2011-01, Vol.108 (4), p.1361-1366

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Many fatal neurodegenerative diseases such as Alzheimer's, Parkinson, the prion-related diseases, and non-neurodegenerative disorders such as type II diabetes are characterized by abnormal amyloid fiber aggregates, suggesting a common mechanism of pathogenesis. We have discovered that a class of systematically designed natural tri- to hexapeptides...

Alternative Titles

Full title

Natural tri- to hexapeptides self-assemble in water to amyloid β-type fiber aggregates by unexpected α-helical intermediate structures

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmed_primary_21205900

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmed_primary_21205900

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1014796108

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