Recent advances in coiled-coil peptide materials and their biomedical applications

Jorgensen, Michael D.; Chmielewski, Jean

doi:10.1039/d2cc04434j

Cited by 14 publications

(17 citation statements)

References 114 publications

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“…As such, several immobilization strategies have been developed for the decoration of biomaterials with proteins . These include protein adsorption directly on the biomaterial surface, , covalent grafting of the proteins, − as well as the design of chimeric proteins harboring bioengineered tags to promote capture on surfaces decorated with the complementary tag binder. , For this strategy, many interacting pairs have been reported: biotin/(strept)avidin, , Fc domain/protein A or G, , heparin-binding domain/heparin, , SH3 domain/peptide binding partners, , and natural or de novo designed coiled-coil peptidic heteromers. , …”

Section: Introductionmentioning

confidence: 99%

“…10,11 For this strategy, many interacting pairs have been reported: biotin/(strept)avidin, 12,13 Fc domain/ protein A or G, 14,15 heparin-binding domain/heparin, 16,17 SH3 domain/peptide binding partners, 18,19 and natural or de novo designed coiled-coil peptidic heteromers. 20,21 Among coiled-coils, the bioinspired Ecoil (EVSALEK) 5 and Kcoil (KVSALKE) 5 peptide pair has been successfully used for the oriented capture of bioactive proteins 22 in surface plasmon resonance (SPR) biosensing, 23−25 enzyme-linked immunosorbent assays (ELISA), 26 recombinant protein purification, 27 as well as capture of proteins on cell culture compatible surfaces 28 and hydrogels. 29 the complementary Kcoil partner was covalently grafted onto a surface.…”

Section: Introductionmentioning

confidence: 99%

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Grafting Strategies of Oxidation-Prone Coiled-Coil Peptides for Protein Capture in Bioassays: Impact of Orientation and the Oxidation State

Dégardin,

Gaudreault,

Oliverio

et al. 2023

ACS Omega

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Many biomedical and biosensing applications require functionalization of surfaces with proteins. To this end, the E/K coiled-coil peptide heterodimeric system has been shown to be advantageous. First, Kcoil peptides are covalently grafted onto a given surface. Ecoil-tagged proteins can then be non-covalently captured via a specific interaction with their Kcoil partners. Previously, oriented Kcoil grafting was achieved via thiol coupling, using a unique Kcoil with a terminal cysteine residue. However, cysteine-terminated Kcoil peptides are hard to produce, purify, and oxidize during storage. Indeed, they tend to homodimerize and form disulfide bonds via oxidation of their terminal thiol group, making it impossible to later graft them on thiol-reactive surfaces. Kcoil peptides also contain multiple free amine groups, available for covalent coupling through carbodiimide chemistry. Grafting Kcoil peptides on surfaces via amine coupling would thus guarantee their immobilization regardless of their terminal cysteine's oxidation state, at the expense of the control over their orientation. In this work, we compare Kcoil grafting strategies for the subsequent capture of Ecoil-tagged proteins, for applications such as surface plasmon resonance (SPR) biosensing and cell culture onto protein-decorated substrates. We compare the "classic" thiol coupling of cysteine-terminated Kcoil peptides to the amine coupling of (i) monomeric Kcoil and (ii) dimeric Kcoil−Kcoil linked by a disulfide bond. We have observed that SPR biosensing performances relying on captured Ecoil-tagged proteins were similar for amine-coupled dimeric Kcoil−Kcoil and thiol-coupled Kcoil peptides, at the expense of higher Ecoil-tagged protein consumption. For cell culture applications, Ecoil-tagged growth factors captured on amine-coupled monomeric Kcoil signaled through cell receptors similarly to those captured on thiol-coupled Kcoil peptides. Altogether, while oriented thiol coupling of cysteine-terminated Kcoil peptides remains the most reliable and versatile platform for Ecoil-tagged protein capture, amine coupling of Kcoil peptides, either monomeric or dimerized through a cysteine bond, can offer a good alternative when the challenges and costs associated with the production of monomeric cysteine-tagged Kcoil are too dissuasive for the application.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Grafting Strategies of Oxidation-Prone Coiled-Coil Peptides for Protein Capture in Bioassays: Impact of Orientation and the Oxidation State

Dégardin,

Gaudreault,

Oliverio

et al. 2023

ACS Omega

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“…CC peptides and polypeptides have emerged as programmable, biosynthetic tectons for the rational design and construction of artificial protein‐mimetic systems and architectures 13–25 . CCs, which consists of two or more alpha helices that intertwine to form a left‐handed superhelical coil, are characterized by a seven‐residue heptad repeat that is alphabetically assigned abcdefg (Figure 1).…”

Section: Introductionmentioning

confidence: 99%

“…While current working design rules have brought forth inspirational nanoarchitectures, including de novo protein polyhedral cages, 13 the expansion of CC design rules remains a critical step towards increasing the complexity and function of these architectures for potential applications in nanomedicine and nanobiotechnology. 13,22,46,[54][55][56] Here, we establish a "minimalistic" set of short, orthogonal CC peptides and employ molecular dynamics (MD) simulations to help provide structural explanations for the experimental binding data. We aimed for a CC set that (1) consists of the minimum length required for forming stable CCs with melting temperature (T m ) values between 30 C and 60 C (an intermediate range that is suitable for dynamic interactions); (2) displays high partner fidelity; and (3) is amenable to analysis by MD simulation to help design potential derivative sequences for incorporation into the CC set.…”

mentioning

confidence: 99%

Interhelical E@g‐N@a interactions modulate coiled coil stability within a de novo set of orthogonal peptide heterodimers

Perez,

Lee,

Colvin

et al. 2023

Journal of Peptide Science

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The designability of orthogonal coiled coil (CC) dimers, which draw on well‐established design rules, plays a pivotal role in fueling the development of CCs as synthetically versatile assembly‐directing motifs for the fabrication of bionanomaterials. Here, we aim to expand the synthetic CC toolkit through establishing a “minimalistic” set of orthogonal, de novo CC peptides that comprise 3.5 heptads in length and a single buried Asn to prescribe dimer formation. The designed sequences display excellent partner fidelity, confirmed via circular dichroism (CD) spectroscopy and Ni‐NTA binding assays, and are corroborated in silico using molecular dynamics (MD) simulation. Detailed analysis of the MD conformational data highlights the importance of interhelical E@g‐N@a interactions in coordinating an extensive 6‐residue hydrogen bonding network that “locks” the interchain Asn‐Asn′ contact in place. The enhanced stability imparted to the Asn‐Asn′ bond elicits an increase in thermal stability of CCs up to ~15°C and accounts for significant differences in stability within the collection of similarly designed orthogonal CC pairs. The presented work underlines the utility of MD simulation as a tool for constructing de novo, orthogonal CCs, and presents an alternative handle for modulating the stability of orthogonal CCs via tuning the number of interhelical E@g‐N@a contacts. Expansion of CC design rules is a key ingredient for guiding the design and assembly of more complex, intricate CC‐based architectures for tackling a variety of challenges within the fields of nanomedicine and bionanotechnology.

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“…Coiled-coil peptides were selected as the building blocks to construct one-dimensional (1D) cell-surface extensions. Various fibrous and tubular nanostructures − have been assembled from coiled-coil-based peptide protomers through site-specific hydrophobic and electrostatic interactions, − metal ion coordination, , and covalent cross-linking. − The peptides that form dimeric coiled coils have been systematically studied, with elucidated correlations between thermal stability (reflecting dimerization affinity) of the dimers and peptide chain length and residue positions. − It would therefore be possible to form the 1D nanostructures through peptide dimerization with tailorable stabilities and tune the assembly and disassembly behaviors through temperature. In this study, we took advantage of the programmable peptide dimerization to construct fibrous cell-surface extensions with different thermal stabilities.…”

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confidence: 99%

Reassembly of Peptide Nanofibrils on Live Cell Surfaces Promotes Cell–Cell Interactions

et al. 2023

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Nature regulates cellular interactions through the cell-surface molecules and plasma membranes. Despite advances in cell-surface engineering with diverse ligands and reactive groups, modulating cell–cell interactions through scaffolds of the cell-binding cues remains a challenging endeavor. Here, we assembled peptide nanofibrils on live cell surfaces to present the ligands that bind to the target cells. Surprisingly, with the same ligands, reducing the thermal stability of the nanofibrils promoted cellular interactions. Characterizations of the system revealed a thermally induced fibril disassembly and reassembly pathway that facilitated the complexation of the fibrils with the cells. Using the nanofibrils of varied stabilities, the cell–cell interaction was promoted to different extents with free-to-bound cell conversion ratios achieved at low (31%), medium (54%), and high (93%) levels. This study expands the toolbox to generate desired cell behaviors for applications in many areas and highlights the merits of thermally less stable nanoassemblies in designing functional materials.

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Recent advances in coiled-coil peptide materials and their biomedical applications

Abstract: Extensive research has gone into deciphering the sequence requirements for peptides to fold into coiled-coils of varying oligomeric states. More recently, additional signals have been introduced within coild-coils to promote...

Cited by 14 publications

References 114 publications

Grafting Strategies of Oxidation-Prone Coiled-Coil Peptides for Protein Capture in Bioassays: Impact of Orientation and the Oxidation State

Grafting Strategies of Oxidation-Prone Coiled-Coil Peptides for Protein Capture in Bioassays: Impact of Orientation and the Oxidation State

Interhelical E@g‐N@a interactions modulate coiled coil stability within a de novo set of orthogonal peptide heterodimers

Reassembly of Peptide Nanofibrils on Live Cell Surfaces Promotes Cell–Cell Interactions

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