@article {14742,
	title = {Affinity-triggered assemblies based on a designed peptide-peptide affinity pair},
	journal = {Biotechnology Journal},
	volume = {-},
	year = {2019},
	pages = {-},
	abstract = {<p>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 was 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 were produced chemically and conjugated to multivalent polyethylene glycol, yielding two components. Upon mixing, they together form soft biocompatible affinity-triggered assemblies, stable in stem cell culture media, and displaying mechanical properties in the same order of magnitude as for those hydrogels formed with the full WW protein in tandem.</p>
},
	url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/biot.201800559},
	author = {Cl{\'a}udia Fernandes and Ana S Pina and Arm{\'e}nio J.M. Barbosa and In{\^e}s Padr{\~a}o and Filipa Duarte and C{\'a}tia Andreia and Silva Teixeira and Vitor Alves and Paula Gomes and Tiago G. Fernandes and Ana M G C Dias and Roque, Ana C A}
}
