Enzyme-Triggered Self-Assembly of Peptide Hydrogels via Reversed Hydrolysis

Toledano, Sophie; Williams, Richard J.; Jayawarna, Vineetha; Ulijn, Rein V.

doi:10.1021/ja056549l

Cited by 481 publications

(417 citation statements)

References 24 publications

(29 reference statements)

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“…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].…”

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confidence: 99%

Redox modulated hydrogelation of a self-assembling short peptide amphiphile

Cao

Fan

et al. 2012

Chin. Sci. Bull.

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Hydrogels resulting from the self-assembly of small peptides are smart nanobiomaterials as their nanostructuring can be readily tuned by environmental stimuli such as pH, ionic strength and temperature, thereby favoring their practical applications. This work reports experimental observations of formation of peptide hydrogels in response to the redox environment. Ac-I 3 K-NH 2 is a short peptide amphiphile that readily self-assembles into long nanofibers and its gel formation occurs at concentrations of about 10 mmol/L. Introduction of a Cys residue into the hydrophilic region leads to a new molecule, Ac-I 3 CGK-NH 2 , that enables the formation of disulfide bonds between self-assembled nanofibers, thus favoring cross-linking and promoting hydrogel formation. Under oxidative environment, Ac-I 3 CGK-NH 2 formed hydrogels at much lower concentrations (even at 0.5 mmol/L). Furthermore, the strength of the hydrogels could be easily tuned by switching between oxidative and reductive conditions and time. However, AFM, TEM, and CD measurements revealed little morphological and structural changes at molecular and nano dimensions, showing no apparent influence arising from the disulfide bond formation.peptide amphiphiles, self-assembly, hydrogelation, redox stimuli Citation:Cao C H, Cao M W, Fan H M, et al. Redox modulated hydrogelation of a self-assembling short peptide amphiphile.

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confidence: 99%

Redox modulated hydrogelation of a self-assembling short peptide amphiphile

Cao

Fan

et al. 2012

Chin. Sci. Bull.

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“…Histidine H (1c) or -ve: Glutamic Acid E (1d); Aspartic Acid D (1e); Cysteic Acid CA (1f)) with different side chain pKa values ( Table 1) were incubated individually with four-fold excess (based on previous protocols, see 20,34 ) of phenylalanine-NH2 (F-NH2, 2) at varying concentrations (Table S1) in the presence of thermolysin (1 mg.ml -1 ), in 100 mM sodium phosphate buffer pH 7.4 , Figure 1.…”

Section: Resultsmentioning

confidence: 99%

Sequence Adaptive Peptide–Polysaccharide Nanostructures by Biocatalytic Self-Assembly

Abul‐Haija

Ulijn

2015

Biomacromolecules

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Co-assembly of peptides and polysaccharides can give rise to formation of nanostructures with tunable morphologies. We show that in situ enzymatic exchange of a dipeptide sequences in aromatic peptide amphiphiles/polysaccharide co-assemblies enables dynamic formation and degradation of different nanostructures depending on the nature of the polysaccharide present. This is achieved in a one-pot system composed of Fmoc-cystic acid (CA), Fmoc-lysine (K) plus phenylalanine amide (F) in the presence of thermolysin which, through dynamic hydrolysis and amide formation gives rise to dynamic peptide library composed of the corresponding Fmocdipeptides (CAF and KF). When the cationic polysaccharide chitosan is added to this mixture, selective amplification of the CAF peptide is observed giving rise to formation of nanosheets through co-assembly. By contrast, upon addition of anionic heparin, KF is formed which gives rise to a nanotube morphology. The dynamic adaptive potential was demonstrated by sequential morphology changes depending on the sequence of polysaccharide addition. This first demonstration of the ability to access different peptide sequences and nanostructures depending on presence of biopolymers may pave the way to biomaterials that can adapt their structure and function and may be of relevance in design of materials able to undergo dynamic morphogenesis.

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“…[148] Hydrogels may be prepared in aqueous solutions by UV [149] or thermo-initiated radical polymerization, [150] addition reaction, [151] self-assembly of recognition motifs such as coiled-coils, [152,153] peptides, [154][155][156] hydrogen-bridges, [157] or DNA. [158,159] These methods can be used in a huge number of particular techniques for the manufacture of strange hydrogel assemblies that are particularly useful for sensing.…”

Section: Drug Loading and Releasementioning

confidence: 99%

Insight into hydrogels

Khan

Ullah

et al. 2016

Designed Monomers and Polymers

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The development and introduction of injectable biomaterials and the identification of methods through which materials may form in situ are currently the topics of interest in materials science, specifically in the field of biomaterials. Over the last few decades, hydrogels which refers to the swellable polymeric matrices have gained wide attention due to their excellent characteristics such as swelling in different media, pH and temperature sensitivity, and sensitivity to other stimuli. Nowadays, injectable hydrogels have widely been studied due to their excellent insitu gelation at body temperature. These injectable insitu gels serve as depot system which ensures the local and systemic drug and gene delivery. These insitu gels also protect the proteins and peptide drugs invivo from environmental effect. The current review is made to report latest extensive literature regarding hydrogels, their classification, synthesis methods, structure of hydrogel network, methods of crosslinking, environment-sensitive hydrogel system, drug loading, and release, hydrogels as biosensors and applications of hydrogels.

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Enzyme-Triggered Self-Assembly of Peptide Hydrogels via Reversed Hydrolysis

Abstract: We demonstrate that proteases can be used to selectively trigger the self-assembly of peptide hydrogels via reversed hydrolysis.

Cited by 481 publications

References 24 publications

Redox modulated hydrogelation of a self-assembling short peptide amphiphile

Redox modulated hydrogelation of a self-assembling short peptide amphiphile

Sequence Adaptive Peptide–Polysaccharide Nanostructures by Biocatalytic Self-Assembly

Insight into hydrogels

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