Supramolecular Hydrogel of a d-Amino Acid Dipeptide for Controlled Drug Release in Vivo

Abstract

A supramolecular hydrogel based on D-amino acids, which resists hydrolysis catalyzed by proteinase K and offers long-term biostability, exhibits controlled release in vivo, as proved by the pharmacokinetics of encapsulated 125I tracers and the SPECT imaging of the hydrogel-encapsulated 131I tracers. As the first in vivo imaging investigation of the drug release properties of the supramolecular hydrogel, isotope encapsulation serves as a valid, useful assay for characterizing the controlled release properties of supramolecular hydrogels in vivo. Our results indicate that supramolecular hydrogels promise new biomaterials for controlled drug release.

Developing a self-healing supramolecular nucleoside hydrogel

“…[1][2][3] There already exist examples of low molecular weight gelating entities with potential for use in drug delivery, whether they be therapeutic molecular gels, such as the recent linifinib 4 and benzothiazole 5 examples or inert gelator matrices such as the extensively studied tri-/dipeptide gelators. [6][7][8] Whilst there is extensive literature describing the applications of LMWGs in drug delivery, there are only a few published examples of these inert matrix gelators that possess self-healing properties i.e. the ability to reform after application of high shear.…”

Terminal Is Important for the Helicity of the Self-Assemblies of Dipeptides Derived from Alanine

“…27 For the D-amino acid dipeptides, they showed excellent biostability against proteinase K in vitro. 12 Generally, the dipeptides can self-assemble into varieties of nanostructures, such as spherical vesicles, nanotubes, and nanowires through π−π stackings, hydrophobic associations, electrostatic interactions, and H-bondings. [2][3][4]6,13 Helicity is believed to have a strong relationship with the origin of life.…”

The enzyme-instructed assembly of the core of yeast prion Sup35 to form supramolecular hydrogels

“…This result agrees with that D-peptide resists proteolytic degradation. 49 On the contrary, precursors made of L-amino acids, L- 3P and L- 4P , almost completely degrade after the incubation with proteinase K for 24 h. We only detect the fragment N'F for the degradation of L- 3P . While N'F, N'FG and N'FGN coexist as the fragments for the degradation of L- 4P at the beginning of incubation with proteinase K. Based on that only 1.1 % L- 4P remains at 1h, and 19.6 % L- 3P at 1h, we speculate that the number of phenylalanine also plays a role in the biostability of precursors.…”