Towards open-ended evolution in self-replicating molecular systems

• Herman Duim and
• Sijbren Otto

Beilstein J. Org. Chem. 2017, 13, 1189–1203, doi:10.3762/bjoc.13.118

• enhanced by electrostatic interactions between amino acids residing on the c and g positions of the α-helices. Ghadiri et al. showed that such coiled-coil peptides are capable of self-replication [35]. As depicted in Figure 7, helical polypeptides can act as a template for shorter peptide fragments by

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

• assembly [9]. Peptide-based nanoparticle aggregation was demonstrated first by Woolfson and coworkers by means of coiled-coil peptides that were immobilized on the nanoparticle surface [26]. Reversibility of the assembly formation, a key feature of a switchable system, has thus far been explored only for a

• in pH results in disruption of the fibers and coiled-coil peptides are formed again. A subsequent decrease of the pH to 9 led to a dramatic change in the morphology of the peptide–nanoparticle assemblies. Whereas long and relatively thin nanoparticle-decorated fibers were observed prior to the change