3 research outputs found
Exploiting oligo(amido amine) backbones for the multivalent presentation of coiled-coil peptides
The investigation of coiled coil formation for one mono- and two divalent peptide-polymer conjugates is presented. Through the assembly of the full conjugates on solid support, monodisperse sequence-defined conjugates are obtained with defined positions and distances between the peptide side chains along the polymeric backbone. A heteromeric peptide design was chosen, where peptide K is attached to the polymer backbone and coiled coil formation is only expected through complexation with the complementary peptide E. Indeed, the monovalent peptide K-polymer conjugate displays rapid coiled coil formation when mixed with the complementary peptide E sequence. The divalent systems show intramolecular homomeric coiled coil formation on the polymer backbone despite the peptide design. Interestingly, this intramolecular assembly undergoes a conformational rearrangement by the addition of the complementary peptide E leading to the formation of heteromeric coiled coil-polymer aggregates. The polymer backbone acts as a template bringing the covalently bound peptide strands in close proximity to each other, increasing the local concentration and inducing the otherwise non-favorable formation of intramolecular helical assemblies
Exploiting Oligo(amido amine) Backbones for the Multivalent Presentation of Coiled-Coil Peptides
Exploiting Oligo(amido amine) Backbones for the Multivalent Presentation of Coiled-Coil Peptides
The
investigation of coiled coil formation for one mono- and two
divalent peptide–polymer conjugates is presented. Through the
assembly of the full conjugates on solid support, monodisperse sequence-defined
conjugates are obtained with defined positions and distances between
the peptide side chains along the polymeric backbone. A heteromeric
peptide design was chosen, where peptide K is attached to the polymer
backbone, and coiled-coil formation is only expected through complexation
with the complementary peptide E. Indeed, the monovalent peptide K-polymer
conjugate displays rapid coiled-coil formation when mixed with the
complementary peptide E sequence. The divalent systems show intramolecular
homomeric coiled-coil formation on the polymer backbone despite the
peptide design. Interestingly, this intramolecular assembly undergoes
a conformational rearrangement by the addition of the complementary
peptide E leading to the formation of heteromeric coiled coil–polymer
aggregates. The polymer backbone acts as a template bringing the covalently
bound peptide strands in close proximity to each other, increasing
the local concentration and inducing the otherwise nonfavorable formation
of intramolecular helical assemblies