Macromolecular Rapid Communications, Vol.35, No.2, 180-185, 2014
Topology- Dependent Swichability of Peptide Secondary Structures in Bioconjugates with Complex Architectures
Peptide sequences, which exhibit a reversible pH-responsive coil to -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.