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 journalArticle

Abstract

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
Volume14
Issue number11
DOIs
Publication statusPublished - 1 Nov 2019

Fingerprint

Hydrogels
Peptides
Proline
Culture Media
Stem Cells
Cell Culture Techniques
Ligands
Proteins
proline transport protein

Keywords

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

Cite this

@article{e0e26e94246f42a7a49517d89a1f2e79,
title = "Affinity-Triggered Assemblies Based on a Designed Peptide–Peptide Affinity Pair",
abstract = "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.",
keywords = "affinity interactions, physical hydrogels, protein materials, self-assembly, WW domains",
author = "Fernandes, {Cl{\'a}udia S. M.} and Pina, {Ana S.} and Barbosa, {Arm{\'e}nio J. Moura} and In{\^e}s Padr{\~a}o and Filipa Duarte and Teixeira, {C{\'a}tia A. S.} and V{\'i}tor Alves and Paula Gomes and Fernandes, {Tiago G.} and Dias, {Ana M. G. Carvalho} and Roque, {Ana C. A.}",
note = "This work was financed by FCT/MEC (UID/Multi/04378/2019, UID/QUI/50006/2019, and UID/AGR/04129/2013) and cofinanced by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007728). The authors thank FCT/MEC for the research fellowship SFRH/BPD/97585/2013 for A.S.P., SFRH/BPD/112543/2015 for A.J.M.B., and PD/BD/105871/2014 for C.S.M.F. The authors would like to acknowledge the Laboratorio de Analises (FCT-NOVA) for the ICP analysis and the BioLab (FCT-NOVA) for the CD spectroscopy and Microscale Thermophoresis studies.",
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month = "11",
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Affinity-Triggered Assemblies Based on a Designed Peptide–Peptide Affinity Pair. / Fernandes, Cláudia S. M.; Pina, Ana S.; Barbosa, Arménio J. Moura; Padrão, Inês; Duarte, Filipa; Teixeira, Cátia A. S.; Alves, Vítor; Gomes, Paula; Fernandes, Tiago G.; Dias, Ana M. G. Carvalho; Roque, Ana C. A.

In: Biotechnology Journal, Vol. 14, No. 11, 1800559, 01.11.2019.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Affinity-Triggered Assemblies Based on a Designed Peptide–Peptide Affinity Pair

AU - Fernandes, Cláudia S. M.

AU - Pina, Ana S.

AU - Barbosa, Arménio J. Moura

AU - Padrão, Inês

AU - Duarte, Filipa

AU - Teixeira, Cátia A. S.

AU - Alves, Vítor

AU - Gomes, Paula

AU - Fernandes, Tiago G.

AU - Dias, Ana M. G. Carvalho

AU - Roque, Ana C. A.

N1 - This work was financed by FCT/MEC (UID/Multi/04378/2019, UID/QUI/50006/2019, and UID/AGR/04129/2013) and cofinanced by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007728). The authors thank FCT/MEC for the research fellowship SFRH/BPD/97585/2013 for A.S.P., SFRH/BPD/112543/2015 for A.J.M.B., and PD/BD/105871/2014 for C.S.M.F. The authors would like to acknowledge the Laboratorio de Analises (FCT-NOVA) for the ICP analysis and the BioLab (FCT-NOVA) for the CD spectroscopy and Microscale Thermophoresis studies.

PY - 2019/11/1

Y1 - 2019/11/1

N2 - 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.

AB - 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.

KW - affinity interactions

KW - physical hydrogels

KW - protein materials

KW - self-assembly

KW - WW domains

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