Higher and lower supramolecular orders for the design of self-assembled heterochiral tripeptide hydrogel biomaterials

Marchesan, Silvia; Styan, Katie E.; Easton, Christopher D.; Waddington, Lynne J.; Vargiu, Attilio Vittorio

doi:10.1039/c5tb00858a

Cited by 89 publications

(100 citation statements)

References 43 publications

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“…The observed peaks of RFFFR are located in the range in which n→π* transitions typically occur and are relatively broad. However, very similar CD spectra of other short self‐assembling peptides and other aromatic systems have been observed before and assigned as π→π* transitions . Furthermore, the peak positions are red‐shifted as a function of higher peptide concentrations.…”

Section: Resultssupporting

confidence: 74%

The Physical Properties and Self‐Assembly Potential of the RFFFR Peptide

2016

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The self-assembly of fibers from peptides has attracted a tremendous amount of attention due to its many applications, such as in drug-delivery systems, in tissue engineering, and in electronic devices. Recently, the self-assembly potential of the designer peptide RFFFR has been reported. Here it is experimentally verified that the peptide forms fibers that are entangled and form solid spheres without water inside. Upon dilution below the critical fiber concentration, the fibers untangle and become totally separated prior to dissolution. These structures readily bind thioflavin T, resulting in a characteristic change in fluorescent properties consistent with β-sheet-rich amyloid structures with aromatic/hydrophobic grooves. The circular dichroism spectroscopy data are dominated by a π→π* transition, thus indicating that the fibers are stabilized by π-stacking. Contrary to what was expected, the dissolution of the spheres/fibers results in increasing fluorescence anisotropy over time. This is explained in terms of HomoFRET between phenylalanine residues with a T-shaped π-stacking mode, which was determined in another study to be the dominant mode through atomistic simulations and semiempirical calculations. Kelvin probe force microscopy measurements indicate that the spheres and fibers have a conductivity comparable to that of gold. Hence, these self-assembled structures might be applicable in organic solid-state electronic devices. The dissolution properties of the spheres further suggest that they might be used as drug-delivery systems.

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Section: Resultssupporting

confidence: 74%

The Physical Properties and Self‐Assembly Potential of the RFFFR Peptide

2016

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“…A second, narrow endotherm with a minimum just above 100 °C could be ascribed to the evaporation of residual buffer solution. It is worth noting that the DSC data of similar peptides and amyloids often display multiple minima that are not always discernible and result in wide, asymmetric endotherms; besides the gel-to-sol transition, other minima in the range of 80–85 °C can be ascribed to aggregates formed during heating [ 41 – 42 ]. It is thus possible that the wide endotherm observed in this work is the sum of all such different components.…”

Section: Resultsmentioning

confidence: 99%

Luminescent supramolecular hydrogels from a tripeptide and nitrogen-doped carbon nanodots

Cringoli¹,

Kralj²,

Kurbasic³

et al. 2017

Beilstein J. Nanotechnol.

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The combination of different components such as carbon nanostructures and organic gelators into composite nanostructured hydrogels is attracting wide interest for a variety of applications, including sensing and biomaterials. In particular, both supramolecular hydrogels that are formed from unprotected D,L-tripeptides bearing the Phe-Phe motif and nitrogen-doped carbon nanodots (NCNDs) are promising materials for biological use. In this work, they were combined to obtain luminescent, supramolecular hydrogels at physiological conditions. The self-assembly of a tripeptide upon application of a pH trigger was studied in the presence of NCNDs to evaluate effects at the supramolecular level. Luminescent hydrogels were obtained whereby NCND addition allowed the rheological properties to be fine-tuned and led to an overall more homogeneous system composed of thinner fibrils with narrower diameter distribution.

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“…Amino acid chirality, considered a key tool to drive peptide self-assembly, exploited at the molecular and supramolecular levels for D-and L-amino acids positions in case of gelling tripeptides has been reported by Marchesan et al (2015a), to establish a higher or lower supramolecular order. So, a suitable design of the chirality in sequence of self-assemblies has been suggested to assign and fine-tune the properties of reported tripeptide gel biomaterials.…”

Section: Tripeptides As Biologics Carriersmentioning

confidence: 99%

Ultrashort Peptide Self-Assembly: Front-Runners to Transport Drug and Gene Cargos

Gupta

Singh

Sharma

et al. 2020

Front. Bioeng. Biotechnol.

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The translational therapies to promote interaction between cell and signal come with stringent eligibility criteria. The chemically defined, hierarchically organized, and simpler yet blessed with robust intermolecular association, the peptides, are privileged to make the cutoff for sensing the cell-signal for biologics delivery and tissue engineering. The signature service and insoluble network formation of the peptide self-assemblies as hydrogels have drawn a spell of research activity among the scientists all around the globe in the past decades. The therapeutic peptide market players are anticipating promising growth opportunities due to the ample technological advancements in this field. The presence of the other organic moieties, enzyme substrates and well-established protecting groups like Fmoc and Boc etc., bring the best of both worlds. Since the large sequences of peptides severely limit the purification and their isolation, this article reviews the account of last 5 years' efforts on novel approaches for formulation and development of single molecule amino acids, ultra-short peptide self-assemblies (di-and tri-peptides only) and their derivatives as drug/gene carriers and tissue-engineering systems.

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Higher and lower supramolecular orders for the design of self-assembled heterochiral tripeptide hydrogel biomaterials

Cited by 89 publications

References 43 publications

The Physical Properties and Self‐Assembly Potential of the RFFFR Peptide

The Physical Properties and Self‐Assembly Potential of the RFFFR Peptide

Luminescent supramolecular hydrogels from a tripeptide and nitrogen-doped carbon nanodots

Ultrashort Peptide Self-Assembly: Front-Runners to Transport Drug and Gene Cargos

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