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RESEARCH PRODUCT
Topology-Dependent Swichability of Peptide Secondary Structures in Bioconjugates with Complex Architectures
Romina I. SütterlinKerstin T. WissPatrick TheatoPatrick TheatoHans G. Börnersubject
chemistry.chemical_classificationPolymers and PlasticsEthylene oxideOrganic ChemistryPeptidePolymerConjugated systemMicroscopy Atomic ForceTopologyCombinatorial chemistryProtein Structure SecondaryPolyethylene Glycolschemistry.chemical_compoundchemistryMaterials ChemistrySelf-assemblyPeptidesProtein secondary structureTopology (chemistry)Conjugatedescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2013-12-09 | Macromolecular Rapid Communications |