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The Conformation of B18 Peptide in the Presence of Fluorinated and Alkylated Nanoparticles
Author(s) -
Rocha Sandra,
Thünemann Andreas F.,
Pereira M. Carmo,
Coelho Manuel A. N.,
Möhwald Helmuth,
Brezesinski Gerald
Publication year - 2005
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200400177
Subject(s) - alkylation , monomer , peptide , nanoparticle , chemistry , fibril , helix (gastropod) , biophysics , beta sheet , stereochemistry , nanotechnology , organic chemistry , materials science , polymer , biochemistry , catalysis , biology , ecology , snail
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.