A Ferrocene–Tryptophan Conjugate: The Role of the Indolic Nitrogen in Supramolecular Assembly

Falcone, Natashya; Basak, Shibaji; Dong, Bin; Syed, Jebriel; Ferranco, Annaleizle; Lough, Alan J.; She, Zhe; Kraatz, Heinz‐Bernhard

doi:10.1002/cplu.201700407

Cited by 23 publications

(11 citation statements)

References 53 publications

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“…The morphology of a nanofiber matrix is reported for both L and D (Figure 4), where we observed long fibers, which showed a three-dimensional interweaving architecture. Fibril structures have been reported as the main morphology of strong peptide based-gel materials [43,44,45,46]. The fibers had an average thickness of 0.056 ± 0.011 μm for MA- l -Phe-OH and 0.058 ± 0.021 μm for MA- d -Phe-OH, which is similar to reported amino acid and peptide hydrogels.…”

Section: Resultssupporting

confidence: 76%

Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels

et al. 2019

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Supramolecular amino acid and peptide hydrogels are functional materials with a wide range of applications, however, their ability to serve as matrices for enzyme entrapment have been rarely explored. Two amino acid conjugates were synthesized and explored for hydrogel formation. These hydrogels were characterized in terms of strength and morphology, and their ability to entrap enzymes while keeping them active and reusable was explored. It was found that the hydrogels were able to successfully entrap two common and significant enzymes—horseradish peroxidase and -amylase—thus keeping them active and stable, along with inducing recycling capabilities, which has potential to further advance the industrial biotransformation field.

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Section: Resultssupporting

confidence: 76%

Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels

et al. 2019

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“…Both interfaces are stabilized by π‐π stacking interactions between the side chains. Although the role of the nitrogen of the indole ring of Trp in self‐assembling has been recently highlighted, taking into account the local context of the Trp side chain and the absence of potential H‐bonding acceptors, this type of interactions cannot directly contribute to the stabilization of W4 assemblies. In conclusion, present findings clearly demonstrate that aromatic residues display a general propensity to form these assemblies despite the significant differences of the physicochemical properties of their side chains.…”

Section: Discussionmentioning

confidence: 99%

Structural Characterization of Self‐Assembled Tetra‐Tryptophan Based Nanostructures: Variations on a Common Theme

et al. 2018

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Over the years, a large number of multidisciplinary investigations has unveiled that the self-assembly of short peptides and even of individual amino acids can generate a variety of different biomaterials. In this framework, we have recently reported that polyethylene glycol (PEG) conjugates of short homopeptides, containing aromatic amino acids such as phenylalanine (Phe, F) and naphthylalanine (Nal), are able to form elongated fibrillary aggregates having interesting chemical and physical properties. We here extend these analyses characterizing the self-assembling propensity of PEG -W4, a PEG adduct of the tetra-tryptophan (W4) sequence. A comprehensive structural characterization of PEG -W4 was obtained, both in solution and at the solid state, through the combination of spectroscopic, microscopic, X-ray scattering and computational techniques. Collectively, these studies demonstrate that this peptide is able to self-assemble in fibrillary networks characterized by a cross β-structure spine. The present findings clearly demonstrate that aromatic residues display a general propensity to induce self-aggregation phenomenon, despite the significant differences in the physicochemical properties of their side chains.

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“…These include a variety of peptide conjugates that exhibit self‐healing and reversible sol‐to‐gel transitions towards sonication that also possess self‐healing properties . A Fc‐dipeptide gelator of Trp‐Trp displays a semi‐Herrick structure in the solid state, referring to the conformation of the two Cp rings and the intramolecular H‐bonding interactions of the two podant peptide chains, with the ability to interact at the supramolecular level (Figure ) …”

Section: Metals and Peptide Gelsmentioning

confidence: 99%

“…[51] A Fc-dipeptide gelator of Trp-Trp displays as emi-Herrick structure in the solid state, referring to the conformation of the two Cp rings andt he intramolecular H-bonding interactions of the two podant peptidec hains, with the ability to interact at the supramolecular level ( Figure 9). [52,53] The bis-substituted Fc conjugate, Fc[CO-Trp-Trp-OMe] 2 ,a ssembles into an organogel that is highly temperature sensitive. In addition, this material displays strong redox sensitivity.O xidation of the Fc results in complete loss of the fibrous network structure, and new spherical assemblies are formed in solution.…”

Section: Ferrocene Peptidesmentioning

confidence: 99%

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Supramolecular Assembly of Peptide and Metallopeptide Gelators and Their Stimuli‐Responsive Properties in Biomedical Applications

Falcone

Kraatz

2018

Chemistry A European J

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Supramolecular gels are a fascinating class of soft materials that have attracted significant attention in recent years. They are composed of small molecule gelators that assemble into supramolecular network structures. The resulting space is filled with solvent. Some gel materials are able to respond to various stimuli making them attractive drug delivery vehicles and as matrices for tissue regeneration. Peptide-based gel materials are particularly attractive as they possess numerous advantages including biocompatibility and biodegradability. Stimuli-responsive peptides that alter properties as a function of pH, redox, temperature, and enzymes offer the potential to create materials with tunable characteristics. In addition, the ability of metal ions to improve the strength of gelation or act as a scaffold has become an interesting approach to develop dynamic peptide gel materials. In this review, the stimuli-responsive properties (pH, redox, temperature, and enzyme responsive properties), as well as the biocompatible/-degradable nature of the peptide gelators are highlighted. In addition, metal ions are discussed as a stimulus to enhance peptide gelation and a number of potential applications of these peptide gelators are provided with an outlook on future directions.

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A Ferrocene–Tryptophan Conjugate: The Role of the Indolic Nitrogen in Supramolecular Assembly

Cited by 23 publications

References 53 publications

Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels

Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels

Structural Characterization of Self‐Assembled Tetra‐Tryptophan Based Nanostructures: Variations on a Common Theme

Supramolecular Assembly of Peptide and Metallopeptide Gelators and Their Stimuli‐Responsive Properties in Biomedical Applications

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