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Affinity‐Triggered Assemblies Based on a Designed Peptide–Peptide Affinity Pair
Author(s) -
Fernandes Cláudia S. M.,
Pina Ana S.,
Moura Barbosa Arménio J.,
Padrão Inês,
Duarte Filipa,
Teixeira Cátia A. S.,
Alves Vítor,
Gomes Paula,
Fernandes Tiago G.,
Carvalho Dias Ana M. G.,
Roque Ana C. A.
Publication year - 2019
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.201800559
Subject(s) - self healing hydrogels , peptide , chemistry , tandem , polyethylene glycol , biophysics , combinatorial chemistry , conjugated system , biocompatible material , protein engineering , ligand (biochemistry) , biochemistry , materials science , receptor , polymer , enzyme , polymer chemistry , biology , organic chemistry , medicine , biomedical engineering , composite material
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.