Single-atom substitution enables supramolecular diversity from dipeptide building blocks

Scarel, Erica; Bellotto, Ottavia; Rozhin, Petr; Kralj, Slavko; Tortora, Mariagrazia; Vargiu, Attilio Vittorio; Zorzi, Rita De; Rossi, Barbara; Marchesan, Silvia

doi:10.1039/d1sm01824h

Cited by 9 publications

(17 citation statements)

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“…When Dox is added to F8 hydrogels, the intensities of the aromatic bands decrease significantly, and a downshift in their positions was observed, pointing toward interactions being present between Dox and the F8 fiber edges. 23 These interactions can be potentially hydrophobic or π–π in nature. In either case, they are weak and unstable as they do not lead to any significant retention of the drug.…”

Section: Resultsmentioning

confidence: 99%

Controlling Doxorubicin Release from a Peptide Hydrogel through Fine-Tuning of Drug–Peptide Fiber Interactions

et al. 2022

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Hydrogels are versatile materials that have emerged in the last few decades as promising candidates for a range of applications in the biomedical field, from tissue engineering and regenerative medicine to controlled drug delivery. In the drug delivery field, in particular, they have been the subject of significant interest for the spatially and temporally controlled delivery of anticancer drugs and therapeutics. Self-assembling peptide-based hydrogels, in particular, have recently come to the fore as potential candidate vehicles for the delivery of a range of drugs. In order to explore how drug–peptide interactions influence doxorubicin (Dox) release, five β-sheet-forming self-assembling peptides with different physicochemical properties were used for the purpose of this study, namely: FEFKFEFK (F8), FKFEFKFK (FK), FEFEFKFE (FE), FEFKFEFKK (F8K), and KFEFKFEFKK (KF8K) (F: phenylalanine; E: glutamic acid; K: lysine). First, Dox-loaded hydrogels were characterized to ensure that the incorporation of the drug did not significantly affect the hydrogel properties. Subsequently, Dox diffusion out of the hydrogels was investigated using UV absorbance. The amount of drug retained in F8/FE composite hydrogels was found to be directly proportional to the amount of charge carried by the peptide fibers. When cation−π interactions were used, the position and number of end-lysine were found to play a key role in the retention of Dox. In this case, the amount of Dox retained in F8/KF8K composite hydrogels was linked to the amount of end-lysine introduced, and an end-lysine/Dox interaction stoichiometry of 3/1 was obtained. For pure FE and KF8K hydrogels, the maximum amount of Dox retained was also found to be related to the overall concentration of the hydrogels and, therefore, to the overall fiber surface area available for interaction with the drug. For 14 mM hydrogel, ∼170–200 μM Dox could be retained after 24 h. This set of peptides also showed a broad range of susceptibilities to enzymatic degradation opening the prospect of being able to control also the rate of degradation of these hydrogels. Finally, the Dox released from the hydrogel was shown to be active and affect 3T3 mouse fibroblasts viability in vitro. Our study clearly shows the potential of this peptide design as a platform for the formulation of injectable or sprayable hydrogels for controlled drug delivery.

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Section: Resultsmentioning

confidence: 99%

Controlling Doxorubicin Release from a Peptide Hydrogel through Fine-Tuning of Drug–Peptide Fiber Interactions

et al. 2022

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“…73 By contrast, the use of fluorophenylalanine at the C-terminus completely altered the supramolecular packing, leading to amphipathic layers – as opposed to water-channels – as revealed by single-crystal XRD. 76…”

Section: Dipeptide Nts and Their Chemical Structuresmentioning

confidence: 99%

Nanotubes and water-channels from self-assembling dipeptides

2023

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“…One is increased hydrophobicity, which can be convenient to induce hydrophobically driven self-organization into nanostructured biomaterials, for instance [26,41,42]. Remarkably, this effect is seen in sequences as short as unprotected dipeptides [43,44] without further structural modifications [45,46].…”

Section: D-amino Acids (D-aa) In Naturementioning

confidence: 99%

Polymer Conjugates of Antimicrobial Peptides (AMPs) with d-Amino Acids (d-aa): State of the Art and Future Opportunities

et al. 2022

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In recent years, antimicrobial peptides (AMPs) have enjoyed a renaissance, as the world is currently facing an emergency in terms of severe infections that evade antibiotics’ treatment. This is due to the increasing emergence and spread of resistance mechanisms. Covalent conjugation with polymers is an interesting strategy to modulate the pharmacokinetic profile of AMPs and enhance their biocompatibility profile. It can also be an effective approach to develop active coatings for medical implants and devices, and to avoid biofilm formation on their surface. In this concise review, we focus on the last 5 years’ progress in this area, pertaining in particular to AMPs that contain d-amino acids, as well as their role, and the advantages that may arise from their introduction into AMPs.

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Single-atom substitution enables supramolecular diversity from dipeptide building blocks

Abstract: Dipeptides are popular building blocks for supramolecular gels that do not persist in the environment and may find various applications. In this work we show that a simple substitution on...

Cited by 9 publications

References 50 publications

Controlling Doxorubicin Release from a Peptide Hydrogel through Fine-Tuning of Drug–Peptide Fiber Interactions

Controlling Doxorubicin Release from a Peptide Hydrogel through Fine-Tuning of Drug–Peptide Fiber Interactions

Nanotubes and water-channels from self-assembling dipeptides

Polymer Conjugates of Antimicrobial Peptides (AMPs) with d-Amino Acids (d-aa): State of the Art and Future Opportunities

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