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Published on: August 1, 2018
Topology-dependent swichability of peptide secondary structures in bioconjugates with complex architectures
Hans G Börner1, Romina I Sütterlin1, Patrick Theato2,3
1Humboldt-Universität zu Berlin, Department of Chemistry, Laboratory for Organic Synthesis of Functional Systems, D-12489, Berlin, Germany.
Abstract:
Peptide sequences, which exhibit a reversible pH-responsive coil to α-helix secondary structure transition, are conjugated to polymer precursors to yield linear AB and graft ABA peptide-poly(ethylene oxide) conjugates. While the PEO B-block is comparable, the conjugates differ in topologies of the peptide bearing A-blocks. The influences of topology on the structure transitions in the peptide segments are investigated, comparing linear AB-bioconjugates with graft ABA-bioconjugates having multiple peptide segments combined in star or pom-pom topologies.
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