Welcome to BörnerLab

Research Overview

  1. Synthesis and design of functional hybrid polymers (bioconjugates)
  2. Bio-mimetic formation of structure and function in synthetic polymers (peptide-guided organization and structure based functions)
  3. Pseudopeptides and precision polymers for biomedical applications (integrated polymer systems for gene or drug delivery)
  4. Bio-functionalization of surfaces (bioactive polymer fibers, scaffolds and material interfaces; Bio-inspired adhesion segments in block copolymers, (bio)-functional coatings, crystal growth modifiers)

Objectives: Controlling interactions in synthetic polymers as precisely as in proteins would have a strong impact on polymer science. Advanced structural and functional control can lead to rational design of, integrated nano- and microstructures. To achieve this, properties of oligopeptides were exploited. By incorporating these as monodisperse segments into synthetic polymers we show how to program structure formation in polymers, control inorganic-organic interfaces in fiber composites, induce structure in biomacromolecules for biomedical applications and generate bioactive surfaces to control biological systems.


22.07.2019 - Learning from peptides to access functional precision polymer sequences
New Paper in Angewandte Chemie has been published and is highlighted as hot article in drug delivery research:

Background: A new strategy to guide the sequence design for accessing functional precision polymers was described. For that purpose, a well-studied peptide that acts as a formulation additive to solubilize a photosensitizer drug was used and the direct translation of side chain functionality sequences towards precision polymer backbones, leads to macromolecules, which mimic drug hosting and release properties of the parent peptide.

Full article Link:


Hot Topic: Drug Delivery:


11.06.2019 - Fish and Clips: A Convenient Strategy to Identify Tyrosinase Substrates with Rapid Activation Behavior for Materials Science Applications
New paper released in ACS Macro Letters:

Background: A Method for the identification of peptides with suitable substrate properties for the enzyme tyrosinase was developed by labeling of enzymatically activated solid-phase supported peptides in a one-bead-one-compound library with a fluorescent probe. This was achieved by Michael addition of a thiol-functionalized probe to dopaquinone residues resulting from enzymatic tyrosine oxidation. Activation kinetics of identified peptides verified the selection process and coating experiments underlined the applicability for materials science.

doi: 10.1021/acsmacrolett.9b00244

04.06.2019 - A strategy to better understand biological adhesion processes
The stick truth about mussel-glue inspired adhesive peptides at the nanomaterial interface

06.05.2019 - Mussel-Glue Inspired Adhesives: A Study on the Relevance of L-Dopa and the Function of the Sequence at Nanomaterial-Peptide Interfaces
New Paper in Advanced Material Interfaces has been published

A mussel-glue inspired peptide obtained via phage display screening mimics aspects of mussel glue proteins by undergoing distinct structural responses at the nanomaterial interface to optimize binding kinetics and surface contacts. NMR in combination with molecular dynamics simulation provides molecular level insights into the structure of the surface- bound adhesive peptide and enables to suggest an adhesion process.

doi: 10.1002/admi.201900501
15.10.2018 - Kekulé Fellowship of the VCI

We congratulate Jana Kohn for receiving the Kekulé Fellowship of the VCI for two years. She will work on an enzyme-free route towards synthetic mussel-inspired polymers.
11.07.2018 - On the way to precision formulation additives: 2D-screening to select solubilizers with tailored host and release capabilities
New Paper in Journal of Controlled Release

Background: A 2-dimensional high-throughput screening method is presented to select peptide sequences from large peptide libraries for precision formulation additives, having a high capacity to specifically host a drug of interest and provide tailored drug release properties. The identified sequences are conjugated with poly(ethylene glycol) (PEG) to obtain peptide-PEG conjugates that proved to be valuable as solubilizers for small organic molecule drugs to overcome limitations of poor water-solubility and low bio-availability.

doi: 10.1016/j.jconrel.2018.06.032
01.04.2018 - Humboldt Fellowship for Postdoctoral Researchers

Dr. Sandra Arias has joined the group with an Alexander von Humboldt Fellowship for Postdoctoral Researchers for two years to work in Mussel-inspired adhesives by switchable β-sheet segments. Congratulations!
29.11.2017 - Engineered collagen - a redox switchable framework for tunable assembly and fabrication of biocompatible surfaces
New Paper in ACS Biomaterials Science & Engineering has been published.
Background: Collagen, processed into several morphologies and originating from various sources, has long since been used as a biocompatible material that can assist wound healing and tissue regeneration. With the advent of biotechnology and solidphase peptide synthesis, new possibilities arise to create rationally designed biomaterials based on collagen sequences incorporating new functionalities whilst maintaining the beneficial properties of natural collagen. In this study a new class of synthetic collagen materials is presented, defined by its simplistic core structure and its therefore predictable behavior.

doi: 10.1021/acsbiomaterials.7b00583

16.11.2017 - PEGylated Precision Segments Based on Sequence-Defined Thiolactone Oligomers

New Paper in Macromolecular Rapid Communications has been published.

Background: A straightforward access route to multifunctional block copolymers, combining a poly(ethylene glycol) (PEG) block and a monodisperse segment with discrete monomer sequence based on thiolactone chemistry, is described. Exploiting an inverse conjugation strategy on a PEG preloaded poly(styrene) synthesis resin enables the convenient introduction of a predefined PEG-block at the α-terminus of thiolactone-based sequence-defined oligomers.

doi: 10.1002/marc.201700688

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