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

2019; Wiley; Volume: 14; Issue: 11 Linguagem: Inglês

10.1002/biot.201800559

1860-7314

Cláudia S. M. Fernandes, Ana Sofia Pina, Arménio Jorge Moura Barbosa, Inês Padrão, Filipa Duarte, Cátia Teixeira, Vítor D. Alves, Paula Gomes, Tiago G. Fernandes, Ana Margarida Gonçalves Carvalho Dias, Ana Cecília A. Roque,

Peptidase Inhibition and Analysis

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.