Affinity-Triggered Assemblies Based on a Designed Peptide–Peptide Affinity Pair

Cláudia S. M. Fernandes, Ana S. Pina, Arménio J. Moura Barbosa, Inês Padrão, Filipa Duarte, Cátia A. S. Teixeira, Vítor Alves, Paula Gomes, Tiago G. Fernandes, Ana M. G. Carvalho Dias, Ana C. A. Roque

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


Affinity-triggered assemblies rely on affinity interactions as the driving force to assemble physically crosslinked networks. WW domains are small hydrophobic proteins binding to proline-rich peptides that are typically produced in the insoluble form. Previous works attempted the biological production of the full WW domain in tandem to generate multivalent components for affinity-triggered hydrogels. In this work, an alternative approach is followed by engineering a 13-mer minimal version of the WW domain that retains the ability to bind to target proline-rich peptides. Both ligand and target peptides are produced chemically and conjugated to multivalent polyethylene glycol, yielding two components. Upon mixing together, they form soft biocompatible affinity-triggered assemblies, stable in stem cell culture media, and display mechanical properties in the same order of magnitude as for those hydrogels formed with the full WW protein in tandem.

Original languageEnglish
Article number1800559
JournalBiotechnology Journal
Issue number11
Publication statusPublished - 1 Nov 2019


  • affinity interactions
  • physical hydrogels
  • protein materials
  • self-assembly
  • WW domains


Dive into the research topics of 'Affinity-Triggered Assemblies Based on a Designed Peptide–Peptide Affinity Pair'. Together they form a unique fingerprint.

Cite this