Log in to save to my catalogue

Revisiting the Self-Assembly of Highly Aromatic Phenylalanine Homopeptides

Revisiting the Self-Assembly of Highly Aromatic Phenylalanine Homopeptides

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_72ef42551122489ab2ec19920ccfaec2

Revisiting the Self-Assembly of Highly Aromatic Phenylalanine Homopeptides

About this item

Full title

Revisiting the Self-Assembly of Highly Aromatic Phenylalanine Homopeptides

Author / Creator

Publisher

Switzerland: MDPI

Journal title

Molecules (Basel, Switzerland), 2020-12, Vol.25 (24), p.6037

Language

English

Formats

Publication information

Publisher

Switzerland: MDPI

More information

Scope and Contents

Contents

Diphenylalanine peptide (FF), which self-assembles into rigid tubular nanostructures, is a very short core recognition motif in Alzheimer's disease β-amyloid (Aβ) polypeptide. Moreover, the ability of the phenylalanine (F or Phe)-homopeptides to self-assemble into ordered nanostructures has been proved. Within this context it was shown that the ass...

Alternative Titles

Full title

Revisiting the Self-Assembly of Highly Aromatic Phenylalanine Homopeptides

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_72ef42551122489ab2ec19920ccfaec2

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_72ef42551122489ab2ec19920ccfaec2

Other Identifiers

ISSN

1420-3049

E-ISSN

1420-3049

DOI

10.3390/molecules25246037

How to access this item