Using experimental and computational energy equilibration to understand hierarchical self-assembly of Fmoc-dipeptide amphiphiles

Sasselli, Ivan R.; Pappas, Charalampos G.; Matthews, Emily R.; Wang, T.; Hunt, Neil T.; Ulijn, Rein V.; Tuttle, Tell

doi:10.1039/c6sm01737a

Cited by 32 publications

(65 citation statements)

References 59 publications

(14 reference statements)

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“…A carboxyl group was included as end group in all cases to assure the sole dependence of the nanostructures on the aminoacid sequence. 33 The aqueous subphase was in all cases a diluted HCl solution (pH = 2) to enhance the self-assembly of the Fmoc-dipeptides on the air/water interface. 34 The Fmoc-dipeptides were not located at the air/water interface when using Milli-Q water with almost neutral pH, see SI6.The following dipeptides were able to selfassemble at the air/water interface: Fmoc-CF (Cysteine-Phenylalanine), Fmoc-MF (Methionine-Phenylalanine), and Fmoc-FF (diphenylalanine).…”

Section: Resultsmentioning

confidence: 99%

Unravelling the 2D self-assembly of Fmoc-dipeptides at fluid interfaces

et al. 2018

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Section: Resultsmentioning

confidence: 99%

Unravelling the 2D self-assembly of Fmoc-dipeptides at fluid interfaces

et al. 2018

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“…FTIR spectra (selected portion, for full spectra see Figure S4, Supporting Information) of the Fmoc‐RGD hydrogel ( Figure A) exhibited a peak at 1623 cm −1 for the amide vibration possibly indicating the presence of β‐sheet structure . In the Fmoc‐RGD/chitosan hydrogel (Figure A), the position of this peak remained unchanged, indicating that chitosan did not affect the secondary structure of the peptide.…”

Section: Figurementioning

confidence: 99%

Composite of Peptide‐Supramolecular Polymer and Covalent Polymer Comprises a New Multifunctional, Bio‐Inspired Soft Material

Chakraborty

Ghosh

Schnaider

et al. 2019

Macromol. Rapid Commun.

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Engineering of extracellular matrix (ECM) mimics, with most of the necessary features of a natural ECM, is a crucial requirement for the design of biomaterials. The natural ECM encompasses a 3D network of intertwined protein nanofibers which contains complex biomolecules for communication between cells.[1] Short peptide-based 3D nanostructured supramolecular hydrogels are excellent candidates for ECM mimicry as they provide networks of fibers which resemble the ECM structure. [2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21] Modifications of certain oligopeptide termini with bio-active ligands, aimed to introduce bio-active components into the system, have also been reported. [22][23][24][25] The tripeptide sequence Arg-Gly-Asp (RGD), which was first recognized in fibronectin as an independent cell attachment site, is the most commonly used bio-active ligand. [26] This tri-peptide sequence is recognized by the α v β 3 and α 5 β 1 integrins located in cell membranes, thus facilitating the coupling of the ECM with the cytoskeleton. [27] Owing to these attributes, the RGD ligand has been introduced into supramolecular or polymeric substrates to facilitate cell attachment. [28][29][30][31] Fmoc-RGD [Fmoc = N-(fluorenyl-9-methoxycarbonyl)] is one of the simplest RGD derivatives capable of forming hydrogels with an inter-connected fibrous network. [15,27] Ulijn's group reported Fmoc-RGD based supramolecular hydrogels in neutral aqueous solution by appropriate mixing of two short peptidebased building blocks, Fmoc-FF (F = phenylalanine) and Fmoc-RGD and utilized them as scaffolds for cell culture. [15] They proposed that Fmoc-RGD alone was not able to form β-sheet fibrils, although in the composite gels of Fmoc-FF and Fmoc-RGD (10-30 wt% Fmoc-RGD), signatures of β-sheet structures were found. We later reported flanking of the RGD sequence by aromatic moieties, demonstrating the hydrogelation of RGD derivatives, including Fmoc-FRGD and Fmoc-RGDF. [32] Hamley and co-workers showed that the simple Fmoc-RGD moiety, without any modification or mixing with other hydrogelator peptides, could from nano-fibrous hydrogels. [27] Castelletto and co-workers prepared monoliths of Fmoc-RGD gels at a high peptide concentration of 10 wt% which showed excellent Bio-Inspired Soft MaterialsPeptide-based supramolecular hydrogels are utilized as functional materials in tissue engineering, axonal regeneration, and controlled drug delivery. The Arg-Gly-Asp (RGD) ligand based supramolecular gels have immense potential in this respect, as this tripeptide is known to promote cell adhesion. Although several RGD-based supramolecular hydrogels have been reported, most of them are devoid of adequate resilience and long-range stability for in vitro cell culture. In a quest to improve the mechanical properties of these tripeptide-based gels and their durability in cell culture media, the Fmoc-RGD hydrogelator is non-covalently functionalized with a biocompatible and biodegradable polymer, chitosan, resulting in a composite hydrog...

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“…1b). 24 In the present experiments, thermolysin-NP conjugates were added to a solution of the non-assembling precursors Fmoc-T (20 mM) and F-NH 2 (80 mM) in a glass vial and left to equilibrate. Samples of the mixture were taken at a series of time points for analysis by RP-HPLC to characterize the catalytic conversion.…”

Section: 2gelation Behavior Of Thermolysin Systemmentioning

confidence: 99%

Biocatalytic Self-Assembly on Magnetic Nanoparticles

Conte

Sahoo

Abul‐Haija

et al. 2018

ACS Appl. Mater. Interfaces

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Combining (bio)catalysis and molecular self-assembly provides an effective approach for the production and processing of self-assembled materials by exploiting catalysis to direct the assembly kinetics and hence controlling the formation of ordered nanostructures. Applications of (bio)catalytic self-assembly in biologically interfacing systems and in nanofabrication have recently been reported. Inspired by self-assembly in biological cells, efforts to confine catalysts on flat or patterned surfaces to exert spatial control over molecular gelator generation and nanostructure self-assembly have also emerged. Building on our previous work in the area, we demonstrate in this report the use of enzymes immobilized onto magnetic nanoparticles (NPs) to spatially localize the initiation of peptide self-assembly into nanofibers around NPs. The concept is generalized for both an equilibrium biocatalytic system that forms stable hydrogels and a nonequilibrium system that normally has a preset lifetime. Characterization of the hydrogels shows that self-assembly occurs at the site of enzyme immobilization on the NPs to give rise to gels with a "hub-and-spoke" morphology, where the nanofibers are linked through the enzyme-NP conjugates. This NP-controlled arrangement of self-assembled nanofibers enables both remarkable enhancements in the shear strength of hydrogel systems and a dramatic extension of the hydrogel stability in the nonequilibrium system. We are also able to show that the use of magnetic NPs enables the external control of both the formation of the hydrogel and its overall structure by application of an external magnetic field. We anticipate that the enhanced properties and stimuli-responsiveness of our NP-enzyme system will have applications ranging from nanomaterial fabrication to biomaterials and biosensing.

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Using experimental and computational energy equilibration to understand hierarchical self-assembly of Fmoc-dipeptide amphiphiles

Cited by 32 publications

References 59 publications

Unravelling the 2D self-assembly of Fmoc-dipeptides at fluid interfaces

Unravelling the 2D self-assembly of Fmoc-dipeptides at fluid interfaces

Composite of Peptide‐Supramolecular Polymer and Covalent Polymer Comprises a New Multifunctional, Bio‐Inspired Soft Material

Biocatalytic Self-Assembly on Magnetic Nanoparticles

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