Impact of multivalent charge presentation on peptide–nanoparticle aggregation

• Daniel Schöne,
• Boris Schade,
• Christoph Böttcher and
• Beate Koksch

Beilstein J. Org. Chem. 2015, 11, 792–803, doi:10.3762/bjoc.11.89

• macrostructures. Keywords: coiled-coil peptides; α-helical fibrils; controlled aggregation; gold nanoparticles; multivalency; Introduction In the past few decades metal and semiconductor nanoparticles, including gold nanoparticles, have gained much interest due to their desirable optical, magnetic, and

• differences in the CD spectra at pH 9 of R2A2, R2A3, R2A4, and R2A5, the signal intensity of R1A3 is dramatically decreased. Furthermore, the minimum at 222 nm is increased and this may point to the formation of assemblies containing α-helical fibrils. This is probably a consequence of the formation of

• wavelength of 254 nm. While an electrophoretic mobility of VW05 could be detected only for a high peptide concentration of 100 µM, the peptide band of R1A3 did not show any mobility. This effect could be explained by the formation of α-helical fibrils (vide infra) that are not able to enter the pores of the