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Revisiting the self-assembly of highly aromatic phenylalanine homopeptides

Author
Mayans, E.; Aleman, C.
Type of activity
Journal article
Journal
Molecules (Basel, Switzerland)
Date of publication
2020-12-20
Volume
25
Number
24
First page
6037:1
Last page
6037:25
DOI
10.3390/molecules25246037
URL
https://www.mdpi.com/1420-3049/25/24/6037 Open in new window
Abstract
Diphenylalanine peptide (FF), which self-assembles into rigid tubular nanostructures, is a very short core recognition motif in Alzheimer’s disease ß-amyloid (Aß) 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 assembly preferences of this family of compounds is altered by capping both the N- and C-termini using highly aromatic fluorenyl groups (i.e., fluore...
Keywords
Molecular engineering, Morphological engineering, Nanostructures, Peptides, Staking interactions, Supramolecular chemistry
Group of research
CRnE - Barcelona Research Center in Multiscale Science and Engineering
IMEM CIEFMA-UPC - Innovation in Materials and Molecular Engineering Center for Research in Structural Integrity, Reliability and Micromechanics of Materials
IMEM-BRT - Innovation in Materials and Molecular Engineering - Biomaterials for Regenerative Therapies

Participants