2011
DOI: 10.1002/anie.201006652
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Zinc‐Triggered Hydrogelation of a Self‐Assembling β‐Hairpin Peptide

Abstract: Zinc‐chronized gelling: Selective zinc‐triggered hydrogel formation is realized by the self‐assembly of a de novo designed peptide (see picture). A non‐natural, zinc‐binding aminocarboxylate residue is incorporated into the peptide and is used to trigger folding, assembly, and subsequent gelation.

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Cited by 124 publications
(79 citation statements)
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“…[6] Thus, we decide to explore the potential of nucleopeptides to serve as building blocks for biomaterials. Among many possible choices of the types of materials, we chose to generate hydrogels[7] of nucleopeptides for two simple reasons: (i) supramolecular hydrogels, resulted from molecular self-assembly in water that form entangled nanofibers, have exhibited considerable promises for applications in biomedicine because of the inherent biocompatibility and biodegradability associated with the supramolecular nanofibers;[8] (ii) despite their versatility and importance, small nucleopeptides have been hardly explored for hydrogels. Thus, the primary goal of this work is to design, synthesize, and evaluate molecular hydrogelators[7a, 7b, 9] made of nucleopeptides.…”
mentioning
confidence: 99%
“…[6] Thus, we decide to explore the potential of nucleopeptides to serve as building blocks for biomaterials. Among many possible choices of the types of materials, we chose to generate hydrogels[7] of nucleopeptides for two simple reasons: (i) supramolecular hydrogels, resulted from molecular self-assembly in water that form entangled nanofibers, have exhibited considerable promises for applications in biomedicine because of the inherent biocompatibility and biodegradability associated with the supramolecular nanofibers;[8] (ii) despite their versatility and importance, small nucleopeptides have been hardly explored for hydrogels. Thus, the primary goal of this work is to design, synthesize, and evaluate molecular hydrogelators[7a, 7b, 9] made of nucleopeptides.…”
mentioning
confidence: 99%
“…Peptide self-assembly is driven by the orchestrated interaction of several intermolecular non-covalent forces including hydrogen bonding, π-π stacking, hydrophobic effect and electrostatic interactions. Environmental stimuli including pH [16][17][18][19], ionic strength and/or metal ions [18,[20][21][22], temperature [23], light [24] and enzyme-triggers [25], provide powerful approaches for modulating hydrogelation. Furthermore, introduction of microenvironment-sensitive amino acid residues into peptide sequences is also an important strategy for controlling peptide self-assembly and hydrogelation [9,[26][27][28].…”
mentioning
confidence: 99%
“…[13][14][15][16] Recently, the development of self-assembled oligopeptides as 3D scaffolds for tissue engineering has stimulated the efforts to expand the applications of supramolecular hydrogels including the development of novel biocompatible methods to form the hydrogels. [17][18][19][20][21][22][23][24][25] Since the balance between hydrophobicity and hydrophilicity determines the ability of a small molecule to form a hydrogel, the careful adjustment of the balance would allow the control of self-assembly of small molecules and the formations of supramolecular hydrogels. [26][27][28][29] Although chemical or physical perturbations (e.g., adjusting pH, temperature, ionic strength, and ultrasonic agitation) are the usually used methods to achieve that balance, [2,[30][31][32][33][34][35][36][37][38] enzyme-responsive self-assembly and gelation of the hydrogelators is advantageous for biomedical applications due to the highly efficient catalytic ability of enzymes in mild conditions and the biocompatibility associated with the enzymes.…”
Section: Introductionmentioning
confidence: 99%