Coiled coil peptide-functionalized surfaces for reversible molecular binding

Minelli, Caterina; Liew, Jian X.; Murugesan, Muthu; Andresen, Heiko

doi:10.1039/c3sm50379h

Cited by 18 publications

(26 citation statements)

References 37 publications

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“…However, at 45°C the storage modulus dropped sharply below the loss modulus indicating loss of structural integrity presumably due to the denaturation of the peptide crosslinks (Figure 4b). 47 Interestingly, the gels maintained their structural integrity and showed significant recovery when cycled through multiple high (100%) and low (1%) strain conditions (Figure 4c). This demonstrates that the CC crosslinked gels can be injected under shear without loss of structural integrity, a property useful in many biomedical applications.…”

Section: Rheological Characterizationmentioning

confidence: 93%

Coiled Coil Crosslinked Alginate Hydrogels Dampen Macrophage-Driven Inflammation

Clapacs

O'Neill

Shrimali

et al. 2021

Preprint

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Alginate hydrogels are widely used for tissue engineering and regenerative medicine due to their excellent biocompatibility. A facile and commonly used strategy to crosslink alginate is the addition of Ca2+ that leads to hydrogelation. However, extracellular Ca2+ is a secondary messenger in activating inflammasome pathways following physical injury or pathogenic insult leading to persistent inflammation and scaffold rejection. Here we present graft copolymers of charge complementary heterodimeric coiled coil (CC) peptides and alginate that undergo supramolecular self-assembly to form Ca2+ free alginate hydrogels. The formation of heterodimeric CCs was confirmed using circular dichroism spectroscopy and scanning electron microscopy revealed a significant difference in pore size between Ca2+ and CC crosslinked gels. The resulting hydrogels were self-supporting and display shear-thinning and shear-recovery properties. In response to lipopolysaccharide (LPS) stimulation, peritoneal macrophages and bone marrow derived dendritic cells cultured in the CC crosslinked gels exhibited a 10-fold reduction in secretion of the proinflammatory cytokine IL-1β compared to Ca2+ crosslinked gels. A similar respose was also observed in vivo upon peritoneal delivery of Ca2+ or CC crosslinked gels. Analysis of peritoneal lavage showed that macrophages in mice injected with Ca2+ crosslinked gels display a more inflammatory phenotype compared to macrophages from mice injected with CC crosslinked gels. These results suggest that CC peptides by virtue of their tunable sequence-structure-function relationship and mild gelation conditions are promising alternative crosslinkers for alginate and other biopolymer scaffolds used in tissue engineering.

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Section: Rheological Characterizationmentioning

confidence: 93%

Coiled Coil Crosslinked Alginate Hydrogels Dampen Macrophage-Driven Inflammation

Clapacs

O'Neill

Shrimali

et al. 2021

Preprint

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“…Coiled‐coils (CC), characterized by the heptad repeat ( abcdefg ) n , are useful scaffolds for engineering conformational flexibility, since the free energy difference between various oligomeric states can be very low . Hitherto, CC assemblies responsive to pH, metal ions, light, redox conditions, hydrophobic ligands or phosphorylation have been successfully designed. Additionally, CC strand displacement using peptides with different affinities to guide the exchange of CC assemblies has recently been presented .…”

Section: Methodsmentioning

confidence: 99%

SwitCCh: Metal‐Site Design for Controlling the Assembly of a Coiled‐Coil Homodimer

2018

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Conformational change of proteins in response to chemical or physical signals is the underlying principle of many regulatory and transport mechanisms in biological systems. The ability to design proteins the conformational state of which can be precisely and reversibly controlled would facilitate the development of molecular machines tailored for specific applications. Here we explore metal‐binding site design to engineer a peptide‐based conformational switch called SwitCCh that assembles into a homodimeric coiled‐coil in response to the addition of ZnII ions or low pH. Addition of ZnII promoted formation of a parallel homodimer with an increase in thermal stability by more than 30 °C. The peptide could be reversibly cycled between the coiled‐coil and random conformation. Furthermore, the SwitCCh peptide was orthogonal to the previously developed coiled‐coil dimer set, indicating it could be used for regulated self‐assembly of coiled‐coil based nanostructures and materials.

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“…One interesting phenomenon that can be engineered with peptide-functionalised gold nanoparticles is reversible self-assembly. The aggregation state can be altered from assembled to disassembled by various triggers, including enzyme activity 2,3 , metal-ligand coordination 4 , pH [5][6][7] and temperature 8,9 . The surface plasmon resonance band of GNPs undergoes a red-shift upon nanoparticle aggregation, causing a colour change of the peptide-GNP solution from red to violet.…”

Section: Introductionmentioning

confidence: 99%

Preparation and thermally-induced self-assembly behaviour of elastin-like peptide side-chain polymer-gold nanoparticle (ESP-GNP) hybrids

Zong¹,

Cobb²,

Cameron³

2021

Arkivoc

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Thermoresponsive gold nanoparticles were prepared by conjugation of short pentapeptide sequences, containing the elastin-like peptide (ELP) repeat unit Val-Pro-Gly-Val-Gly (VPGVG), to a well-defined active ester prepolymer, poly(pentafluorophenyl acrylate) (pPFPA), itself prepared by RAFT polymerisation. Polymers with number-average chain lengths of 25, 50, 75 and 100 were prepared. The cloud points of their aqueous solutions was found to decrease with chain length and peptide sequence, and varied from 76 to 42 o C. Circular dichroism indicated that the cloud point behaviour was accompanied by a reversible change in peptide conformation from a random coil to a -turn. The resulting thermoresponsive elastin peptide side-chain polymers (ESPs) were then conjugated to gold nanoparticles (GNPs) by ligand exchange. The resulting ESP-GNPs similarly displayed thermo-reversible aggregation with transition temperature (Tt) values of 65 and 35 o C for ESPs of chain length 75 and 100, respectively.

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Coiled coil peptide-functionalized surfaces for reversible molecular binding

Cited by 18 publications

References 37 publications

Coiled Coil Crosslinked Alginate Hydrogels Dampen Macrophage-Driven Inflammation

Coiled Coil Crosslinked Alginate Hydrogels Dampen Macrophage-Driven Inflammation

SwitCCh: Metal‐Site Design for Controlling the Assembly of a Coiled‐Coil Homodimer

Preparation and thermally-induced self-assembly behaviour of elastin-like peptide side-chain polymer-gold nanoparticle (ESP-GNP) hybrids

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