Varying the hydrophobic spacer to influence multicomponent gelation

Panja, Santanu; Dietrich, Benjamin; Trabold, Adriana; Zydel, Agata; Qadir, Aleena; Adams, Dave J.

doi:10.1039/d1cc02786g

Cited by 16 publications

(32 citation statements)

References 32 publications

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“…Here we show that combination of a dipeptide gelator (compound 1 ) with non‐gelling amphiphiles (compounds 2 – 6 ) can produce gels at low pH whilst the properties of the multicomponent systems are significantly dependent on the hydrophobicity of the non‐gelling component (Figure 1). We have previously shown that Fmoc‐amphiphiles with short alkyl chain (compounds 2 – 4 ) primarily undergo self‐sorting with 1 [9] . Here, we find that, when the amphiphiles are more hydrophobic ( 5 and 6 ), gel formation is driven by co‐assembly.…”

Section: Introductionsupporting

confidence: 54%

“…Dipeptide 1 forms a self‐supported, invertible gel almost instantly (within few seconds) in DMSO/H 2 O (20/80, v/v) (Figure 1, bottom) [9] . The pH of the gel is around 4.3.…”

Section: Resultsmentioning

confidence: 99%

“…Combination of 1 and 2 – 6 individually results a gel in all cases with a pH of 3.1–3.3 (Figure S4). In the multicomponent gels, the ratios of the components were kept the same as optimised in a previous study [9] . Despite the nonaggregation tendency of compounds 2 – 6 in solution, the microstructure and mechanical properties of the multicomponent gels were very dependent on the hydrophobicity of the Fmoc‐amphiphiles.…”

Section: Resultsmentioning

confidence: 99%

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Controlling Self‐Sorting versus Co‐assembly in Supramolecular Gels

et al. 2022

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Supramolecular gels formed by the combination of different organic molecules are of significant interest in the search of new functional materials. When two different molecules are mixed to form gels, the self-assembled fibres can be a result of self-sorting or co-assembly. A key challenge is to control the network type. Here, we demonstrate that control over the network type can be achieved either by varying the hydrophobicity of a component or by employing a pH-switch method.

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Section: Introductionsupporting

confidence: 54%

“…Dipeptide 1 forms a self‐supported, invertible gel almost instantly (within few seconds) in DMSO/H 2 O (20/80, v/v) (Figure 1, bottom) [9] . The pH of the gel is around 4.3.…”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Controlling Self‐Sorting versus Co‐assembly in Supramolecular Gels

et al. 2022

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“…Materials. The 1ThNapFF gelator was synthesized as described previously [ 38 ]. Urease (U4002-100KU, Jack Beans, 100,000 units/g solid) and urea (ultrapure 99%) were purchased from Alfa Aesar.…”

Section: Methodsmentioning

confidence: 99%

Using Rheology to Understand Transient and Dynamic Gels

Bianco

Panja

Adams

2022

Gels

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Supramolecular gels can be designed such that pre-determined changes in state occur. For example, systems that go from a solution (sol) state to a gel state and then back to a sol state can be prepared using chemical processes to control the onset and duration of each change of state. Based on this, more complex systems such as gel-to-sol-to-gel and gel-to-gel-to-gel systems can be designed. Here, we show that we can provide additional insights into such systems by using rheological measurements at varying values of frequency or strain during the evolution of the systems. Since the different states are affected to different degrees by the frequency and/or strain applied, this allows us to better understand and follow the changes in state in such systems.

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“…The self-assembly of peptides is also partially controlled by interactions between hydrophobic amino acid residues, such as associative phenylalanine-phenylalanine (FÀ F) interactions, which are commonly observed in supramolecular peptide hydrogels. [69][70][71] In addition, enzymes can also be used as a stimulus to trigger the self-(dis)assembly in supramolecular hydrogels, and the inherent biocompatibility of peptide-based gels makes them ideal targets for enzymatic cleavage. [72] Moreover, the mild reaction conditions required for enzymatic reactions, as well as the homogeneity of the resulting hydrogels are additional advantages of peptide hydrogels.…”

Section: Small Gelators: Peptidesmentioning

confidence: 99%

Supramolecular Hydrogels: Design Strategies and Contemporary Biomedical Applications

Omar

Ponsford

Dreiss

et al. 2022

Chemistry An Asian Journal

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Self‐assembly of supramolecular hydrogels is driven by dynamic, non‐covalent interactions between molecules. Considerable research effort has been exerted to fabricate and optimise supramolecular hydrogels that display shear‐thinning, self‐healing, and reversibility, in order to develop materials for biomedical applications. This review provides a detailed overview of the chemistry behind the dynamic physicochemical interactions that sustain hydrogel formation (hydrogen bonding, hydrophobic interactions, ionic interactions, metal‐ligand coordination, and host‐guest interactions). Novel design strategies and methodologies to create supramolecular hydrogels are highlighted, which offer promise for a wide range of applications, specifically drug delivery, wound healing, tissue engineering and 3D bioprinting. To conclude, future prospects are briefly discussed, and consideration given to the steps required to ultimately bring these biomaterials into clinical settings.

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Varying the hydrophobic spacer to influence multicomponent gelation

Abstract: Mixing low molecular weight gelators (LMWGs) shows promise as a means of preparing innovative materials with exciting properties. Here, we investigate the effect of increasing hydrophobic chain length on the...

Cited by 16 publications

References 32 publications

Controlling Self‐Sorting versus Co‐assembly in Supramolecular Gels

Controlling Self‐Sorting versus Co‐assembly in Supramolecular Gels

Using Rheology to Understand Transient and Dynamic Gels

Supramolecular Hydrogels: Design Strategies and Contemporary Biomedical Applications

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