Nanostructured Hydrogels for Three‐Dimensional Cell Culture Through Self‐Assembly of Fluorenylmethoxycarbonyl–Dipeptides

Jayawarna, Vineetha; Ali, Murtza; Jowitt, Thomas A.; Miller, Aline F.; Saiani, Alberto; Gough, Julie E.; Ulijn, Rein V.

doi:10.1002/adma.200501522

Cited by 941 publications

(909 citation statements)

References 26 publications

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“…Apart from their pathological relevance, amyloid fibrils are one of several self-assembling peptide systems that are attracting increasing interest for applications ranging from molecular electronics (20,21) to tissue engineering and material science (22)(23)(24)(25)(26)(27). Metallic nanowires have been produced by different strategies on templates made from protein nanotubes and nanofibrils (20,21), and the possibility to control both the vertical and horizontal arrangements of the peptide nanotubes has been demonstrated recently (28).…”

Section: Charge Transport and Intrinsic Fluorescence In Amyloid-likementioning

confidence: 99%

Charge transport and intrinsic fluorescence in amyloid-like fibrils

Mercato

Pompa²,

Maruccio³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

198

199

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Section: Charge Transport and Intrinsic Fluorescence In Amyloid-likementioning

confidence: 99%

Charge transport and intrinsic fluorescence in amyloid-like fibrils

Mercato

Pompa²,

Maruccio³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

198

199

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“…Peptide hydrogels have been actively exploited for a variety of biomedical applications such as cell culture, regenerative medicine, controlled drug and gene delivery [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15]. Most peptide hydrogels arise from the entanglement of selfassembled nanoobjects such as nanofibers and nanotubes.…”

mentioning

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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Section: Introductionmentioning

confidence: 99%

“…1,2 A recent expansion in the number of LMWG systems reported has led to a rapid growth in reports of characterisation and applications of a particular class of this type of molecule, namely aromatic conjugated dipeptide LMWG. [3][4][5][6][7][8] These systems typically consist of a hydrophobic, often aromatic, dipeptide sequences conjugated to Fmoc (9-fluorenylmethoxycarbonyl) 9,10 or naphthalene 3,4 ; further conjugations have also been reported. 11,12 Through the use of an environmental cue, 13 such as an enzymatic trigger, 14 temperature, 15,16 or light 12 some of these conjugates selfassemble into anisotropic fibrils that can eventually cause hydrogelation through the immobilisation of water by the fibrillar network.…”

Section: Introductionmentioning

confidence: 99%

“…17 It is apparent from previous work that two LMWG molecules that differ only by a single amino acid can give rise to hydrogels with dramatically different rheological and phase properties. 3,4,10,18 However, the structural basis for these differences in material properties is not understood.The short-range molecular architecture of some LMWG systems has been studied. For example, the chirality of assembled naphthalene conjugated dipeptides has been reported to correlate to the D-or L-enantiomer of the incorporated amino acids with left-and right-handed assemblies being formed respectively.…”

mentioning

confidence: 99%

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Structural determinants in a library of low molecular weight gelators

et al. 2015

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ARTICLELow molecular weight hydrogels are formed by molecules that form a matrix that immobilises water to form a self-supporting gel. Such gels have uses as biomaterials such as molecular scaffolds and structures for tissue engineering. One class of low molecular weight gelators (LMWG), naphthalene-conjugated dipeptides, has been shown to form hydrogels via selfassembly following a controlled drop in pH. A library of naphthalene-dipeptides has been generated previously although the relationship between the precursor sequence and the resulting self-assembled structures remained unclear. Here, we have investigated the structural details of a set of dipeptide sequences containing alanine (A) and valine (V) conjugated to naphthalene groups substituted with a Br, CN or H at the 6-position. Electron microscopy, circular dichroism and X-ray fibre diffraction shows that these LMWG may be structurally classified by their composition: the molecular packing is determined by the class of conjugate, whilst the chirality of the self-assemblies can be attributed to the dipeptide sequence. This provides insights into the relationship between the precursor sequence and the macromolecular and molecular structures of the fibres that make up the resulting hydrogels. IntroductionThe formation of hydrogels from low molecular weight gelators (LMWG) is a useful route to the production of materials for a wide range of applications. 1, 2 A recent expansion in the number of LMWG systems reported has led to a rapid growth in reports of characterisation and applications of a particular class of this type of molecule, namely aromatic conjugated dipeptide LMWG. 3-8 These systems typically consist of a hydrophobic, often aromatic, dipeptide sequences conjugated to Fmoc (9-fluorenylmethoxycarbonyl) 9, 10 or naphthalene 3, 4 ; further conjugations have also been reported. 11,12 Through the use of an environmental cue, 13 such as an enzymatic trigger, 14 temperature, 15,16 or light 12 some of these conjugates selfassemble into anisotropic fibrils that can eventually cause hydrogelation through the immobilisation of water by the fibrillar network. There are now a large number of systems reported in the literature. 17 It is apparent from previous work that two LMWG molecules that differ only by a single amino acid can give rise to hydrogels with dramatically different rheological and phase properties. 3,4,10,18 However, the structural basis for these differences in material properties is not understood.The short-range molecular architecture of some LMWG systems has been studied. For example, the chirality of assembled naphthalene conjugated dipeptides has been reported to correlate to the D-or L-enantiomer of the incorporated amino acids with left-and right-handed assemblies being formed respectively. 3 Other reports have indicated that proteinaceous additives induce changes to the chiral organisation of the self-assembled hydrogelating molecules. 19 In addition to the plethora of molecular hydrogels with varying material properties available, the...

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Nanostructured Hydrogels for Three‐Dimensional Cell Culture Through Self‐Assembly of Fluorenylmethoxycarbonyl–Dipeptides

Cited by 941 publications

References 26 publications

Charge transport and intrinsic fluorescence in amyloid-like fibrils

Charge transport and intrinsic fluorescence in amyloid-like fibrils

Redox modulated hydrogelation of a self-assembling short peptide amphiphile

Structural determinants in a library of low molecular weight gelators

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