Delivery of Active Peptides by Self-Healing, Biocompatible and Supramolecular Hydrogels

Abstract

Supramolecular and biocompatible hydrogels with a tunable pH ranging from 5.5 to 7.6 lead to a wide variety of formulations useful for many different topical applications compatible with the skin pH. An in vitro viability/cytotoxicity test of the gel components demonstrated that they are non-toxic, as the cells continue to proliferate after 48 h. An analysis of the mechanical properties demonstrates that the hydrogels have moderate strength and an excellent linear viscoelastic range with the absence of a proper breaking point, confirmed with thixotropy experiments. Two cosmetic active peptides (Trifluoroacetyl tripeptide-2 and Palmitoyl tripeptide-5) were successfully added to the hydrogels and their transdermal permeation was analysed with Franz diffusion cells. The liquid chromatography-mass spectrometry (HPLC-MS) analyses of the withdrawn samples from the receiving solutions showed that Trifluoroacetyl tripeptide-2 permeated in a considerable amount while almost no transdermal permeation of Palmitoyl tripeptide-5 was observed.

Controlled Lactonization of o-Coumaric Esters Mediated by Supramolecular Gels

“…For this aim, we prepared some gels using Boc-L-DOPA(Bn) 2 -OH [ 45 , 46 ], a gelator widely used in our research lab ( Figure 2 ) [ 47 ]. This gelator can form a variety of noncovalent interactions (π-π stackings between the aromatic rings and H-bonds in the carbamate and carboxylic acid portions, as illustrated in Figure S1 ) and demonstrated its robustness forming gels under several conditions and in the presence of different fillers [ 10 , 48 , 49 , 50 ].…”

Self‐assembling tripeptide forming water‐bound channels and hydrogels

“…In the last two decades, minimalistic peptides have raised great interest for their capability of self-assembling into nanostructured hydrogels for a variety of applications. 1 The vast majority, 2,3 but not all, [4][5][6][7] of peptide gelators employ amphipathic sequences that typically feature Phe residues to promote the spontaneous organization at low concentrations in water. 8 In particular, sequences as short as two to three amino acids are attractive for their low cost and simplicity of production and for the possibility of easily scaling-up their synthesis also in the liquid phase.…”

Ultrashort Cationic Peptide Fmoc-FFK as Hydrogel Building Block for Potential Biomedical Applications

“…Among all peptide-based architectures (e.g., fibers [3], nanospheres [4], and micelles [5]), hydrogels (HGs) represent highly organized materials in which the network, generated by interconnected fibers, is able to retain, due to the hydrophilic portions of the amide skeleton, large amounts of water [6,7]. Thanks to their capabilities to accommodate active pharmaceutical ingredients (APIs) in their pores and to mimic the extracellular matrix because of their swollen structure, HGs have been successfully tested as drugs or contrast agents' reservoirs and as matrices for tissue engineering applications [8,9]. The chemical, physical and mechanical properties of the hydrogel can be easily modulated by the opportune design of the peptide sequence, since the choice of the length, the amino acid lateral side and the insertion of aromatic or aliphatic groups at the N-terminus have a significant impact on its gelation capability and HG features [10][11][12][13].…”