Zinc‐Triggered Hydrogelation of a Self‐Assembling β‐Hairpin Peptide

Micklitsch, Christopher M.; Knerr, Patrick J.; Branco, Monica C.; Nagarkar, Radhika P.; Pochan, Darrin J.; Schneider, Judith C.

doi:10.1002/ange.201006652

Cited by 48 publications

(37 citation statements)

References 42 publications

(5 reference statements)

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“…These observations suggested the formation of a true hydrogel46. The gels formed with higher amounts of Gd(III) exhibited slightly bigger G’ values (Supplementary Figs S9 and S10), which was consistent with results from Xu and Stupp groups that increasing the concentration of metal ions led to better mechanical property of the gels33. The transmission electron microscopy (TEM) was also used to characterize the nanostructures in the solution and the gel.…”

Section: Resultssupporting

confidence: 86%

“…Successful examples of metal ion-induced supramolecular hydrogelations have been reported. For example, Scheneider and co-workers reported on the zinc-induced formation of a hydrogel that was promising for wound healing33. Xu and Stupp had also used potassium and calcium ions, respectively, to induce the formation of supramolecular hydrogels with adjustable mechanical properties3435.…”

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confidence: 99%

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Gd(III)-induced Supramolecular Hydrogelation with Enhanced Magnetic Resonance Performance for Enzyme Detection

Hua

et al. 2017

Sci Rep

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Here we report a supramolecular hydrogel based on Gd(III)-peptide complexes with dramatically enhanced magnetic resonance (MR) performance. The hydrogelations were formed by adding Gd(III) ion to the nanofiber dispersion of self-assembling peptides naphthalene-Gly-Phe-Phe-Tyr-Gly-Arg-Gly-Asp (Nap-GFFYGRGD) or naphthalene-Gly-Phe-Phe-Tyr-Gly-Arg-Gly-Glu (Nap-GFFYGRGE). We further showed that, by adjusting the molar ratio between Gd(III) and the corresponding peptide, the mechanical property of resulting gels could be fine-tuned. The longitudinal relaxivity (r1) of the Nap-GFFYGRGE-Gd(III) was 58.9 mM−1 S−1, which to our knowledge is the highest value for such peptide-Gd(III) complexes so far. Such an enhancement of r1 value could be applied for enzyme detection in aqueous solutions and cell lysates.

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Section: Resultssupporting

confidence: 86%

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confidence: 99%

Gd(III)-induced Supramolecular Hydrogelation with Enhanced Magnetic Resonance Performance for Enzyme Detection

Hua

et al. 2017

Sci Rep

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“…Peptide self-assembly can also be realized by taking advantage of interactions between metal cations and amino acid residues of the peptides. This was demonstrated with gelation of a β-sheet-rich fibrillar hydrogel with zinc ions 53 . Alginate hydrogels are also shear-thinning and have been studied extensively.…”

Section: Macroscopic Design and Delivery Routesmentioning

confidence: 94%

Designing hydrogels for controlled drug delivery

2016

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Hydrogel delivery systems can leverage therapeutically beneficial outcomes of drug delivery and have found clinical use. Hydrogels can provide spatial and temporal control over the release of various therapeutic agents, including small-molecule drugs, macromolecular drugs and cells. Owing to their tunable physical properties, controllable degradability and capability to protect labile drugs from degradation, hydrogels serve as a platform in which various physiochemical interactions with the encapsulated drugs control their release. In this Review, we cover multiscale mechanisms underlying the design of hydrogel drug delivery systems, focusing on physical and chemical properties of the hydrogel network and the hydrogel–drug interactions across the network, mesh, and molecular (or atomistic) scales. We discuss how different mechanisms interact and can be integrated to exert fine control in time and space over the drug presentation. We also collect experimental release data from the literature, review clinical translation to date of these systems, and present quantitative comparisons between different systems to provide guidelines for the rational design of hydrogel delivery systems.

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“…[5] In this study, we rationally designed a fusion protein with four binding sites and used the proteinpeptide interaction to enhance interactions between selfassembled nanofibers, thus leading to the formation of molecular hydrogels (Figure 1).There are only a few examples of polymeric hydrogels formed by specific protein-peptide interactions. [1] They have shown great potential in fields such as three-dimensional (3D) cell culture [2] and controlled drug delivery.…”

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confidence: 99%

Rational Design of a Tetrameric Protein to Enhance Interactions between Self‐Assembled Fibers Gives Molecular Hydrogels

et al. 2012

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Molecular hydrogels have attracted extensive research interest in recent years because of their inherent properties (e.g., formation by the self-assembly of small molecules and their gel-sol/sol-gel phase transitions can be easily manipulated by external stimulus). [1] They have shown great potential in fields such as three-dimensional (3D) cell culture [2] and controlled drug delivery. [3] During the formation of a molecular hydrogel, a small molecule (molecular hydrogelator) needs to selfassemble into a 3D matrix of nanofibers, nanorods, or nanospheres that can hold water molecules within the cavities of the 3D matrix. To form the 3D matrix, there should be strong or at least medium interactions between self-assembled nanostructures. Otherwise, nanostructures with weak interactions between them will only form dispersions or solutions in the aqueous phase. Actually, there are many examples of this kind of self-assembled system that lack strong interactions between the self-assembled structures. [4] This type of solution/dispersion containing self-assembled nanostructures could change to a hydrogel if the interaction between the nanostructures could be enhanced. For example, several groups have demonstrated that zinc and calcium ions can be used to cross-link self-assembled nanofibers to form molecular hydrogels. [5] In this study, we rationally designed a fusion protein with four binding sites and used the proteinpeptide interaction to enhance interactions between selfassembled nanofibers, thus leading to the formation of molecular hydrogels (Figure 1).There are only a few examples of polymeric hydrogels formed by specific protein-peptide interactions. [6] Specific protein-peptide interaction has also been used to direct selfassembly of peptide nanowires into micrometer-sized crystalline cubes. [7] However, there are no reports about the formation of molecular hydrogels through protein-peptide interactions up to now. As mentioned above, the formation of a 3D matrix is crucial to the formation of molecular hydrogels. To use protein-peptide interactions to enhance interfiber interactions to support 3D structures, fusion proteins with multiple binding sites are needed. These kinds of fusion proteins usually contain two parts, one for multimer formation and the other for peptide binding. However, these fusion proteins are usually in the balance between multimers with multiple binding sites and monomer with only one binding site. The dissociation constants of protein-peptide interactions are also usually in the micro-to millimolar range. It remains a challenge to develop a protein that can predominantly (> 95 %) form multimers with multiple binding sites. It would also be highly interesting for researchers in the field of biomaterials to develop a protein-peptide interaction with Figure 1. Protein-peptide interaction can be used to enhance interactions between self-assembled fibers, thus leading to molecular hydrogelation. A) Chemical structure of Nap-GFFYGGGWRESAI (1: nongelator) with a possible self-assembly a...

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Zinc‐Triggered Hydrogelation of a Self‐Assembling β‐Hairpin Peptide

Cited by 48 publications

References 42 publications

Gd(III)-induced Supramolecular Hydrogelation with Enhanced Magnetic Resonance Performance for Enzyme Detection

Gd(III)-induced Supramolecular Hydrogelation with Enhanced Magnetic Resonance Performance for Enzyme Detection

Designing hydrogels for controlled drug delivery

Rational Design of a Tetrameric Protein to Enhance Interactions between Self‐Assembled Fibers Gives Molecular Hydrogels

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