Secondary Structure-Driven Hydrogelation Using Foldable Telechelic Polymer-Peptide Conjugates

Ronja Otter; Nina Alexandra Henke; Christian Berac; Tobias Bauer; Matthias Barz; Sebastian Seiffert; Pol Besenius

doi:10.1002/marc.201800459

Secondary Structure-Driven Hydrogelation Using Foldable Telechelic Polymer-Peptide Conjugates

Macromol Rapid Commun. 2018 Sep;39(17):e1800459. doi: 10.1002/marc.201800459. Epub 2018 Jul 24.

Authors

Ronja Otter¹, Nina Alexandra Henke¹, Christian Berac¹, Tobias Bauer¹, Matthias Barz¹, Sebastian Seiffert², Pol Besenius¹

Affiliations

¹ Institute of Organic Chemistry, Johannes Gutenberg University Mainz, Duesbergweg 10-14, D-55128, Mainz, Germany.
² Institute of Physical Chemistry, Johannes Gutenberg University Mainz, Duesbergweg 10-14, D-55128, Mainz, Germany.

PMID: 30040152
DOI: 10.1002/marc.201800459

Abstract

The synthesis of ABA and ABA' triblock polyethylene glycol-and polysarcosine-peptide conjugates is reported. The A/A' peptides are based on phenylalanine(F)-histidine(H) pentapeptide sequences FHFHF, which promote pH-switchable β-sheet self-assembly into nanorods in water. Only parallel β-sheet-driven folding and intermolecular assembly using ABA triblock polymer-peptide conjugates leads to interstrand cross-linking and hydrogelation, highlighting the impact of supramolecular interactions-directed structure formation at the nano- and mesoscopic level.

Keywords: hydrogels; peptide conjugation; stimulus-responsive; supramolecular polymers; β-sheets.

MeSH terms

Hydrogels / chemistry*
Hydrogen-Ion Concentration
Molecular Structure
Particle Size
Peptides / chemistry*
Polymers / chemistry*
Surface Properties

Substances

Hydrogels
Peptides
Polymers

Abstract

MeSH terms

Substances

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