Conformation of B18 Peptide in the Presence of Fluorinated and Alkylated Nanoparticles

Refolding the sheets. Fluorinated nanoparticles with a diameter of 4 nm were found to induce α‐helix‐rich structures in the fibril‐forming peptide, B18. In contrast, the alkylated analogues induced aggregation and β‐sheet formation (see CD spectra). Fluorinated particles are proposed to be potential...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2005-02, Vol.6 (2), p.280-283
Main Authors: Rocha, Sandra, Thünemann, Andreas F, Pereira, M. Carmo, Coelho, Manuel A.N, Möhwald, Helmuth, Brezesinski, Gerald
Format: Article
Language:English
Subjects:
Alkylation
Animals
B18 peptide
Circular Dichroism
conformational analysis
fluorine
Fluorine - chemistry
Glycoproteins - chemistry
Molecular Structure
Nanostructures
Peptides - chemistry
Protein Structure, Secondary
Receptors, Cell Surface
Strongylocentrotus purpuratus - chemistry
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Summary:Refolding the sheets. Fluorinated nanoparticles with a diameter of 4 nm were found to induce α‐helix‐rich structures in the fibril‐forming peptide, B18. In contrast, the alkylated analogues induced aggregation and β‐sheet formation (see CD spectra). Fluorinated particles are proposed to be potential candidates for the stabilization of protein monomeric structures.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.200400177