Anthranilamide-based Short Peptides Self-Assembled Hydrogels as Antibacterial Agents

Abstract

In this study, we describe the synthesis and molecular properties of anthranilamide-based short peptides which were synthesised via ring opening of isatoic anhydride in excellent yields. These short peptides were incorporated as low molecular weight gelators (LMWG), bola amphiphile, and C3-symmetric molecules to form hydrogels in low concentrations (0.07–0.30% (w/v)). The critical gel concentration (CGC), viscoelastic properties, secondary structure, and fibre morphology of these short peptides were influenced by the aromaticity of the capping group or by the presence of electronegative substituent (namely fluoro) and hydrophobic substituent (such as methyl) in the short peptides. In addition, the hydrogels showed antibacterial activity against S. aureus 38 and moderate toxicity against HEK cells in vitro.

Stimuli-Responsive Hydrogels for Local Post-Surgical Drug Delivery

“…Anthranilamide-based short peptides formed a self-assembled hydrogel, which was triggered by changes in pH, heat, and solvent. Applying substituents on the capping group and changing the hydrophobicity are the parameters that have significant effects on Anthranilamide based hydrogels [46].…”

Facile construction of a family of supramolecular gels with good levofloxacin hydrochloride loading capacity

“…22 Kumar et al prepared a series of anthranilamide-based hydrogels that showed antibacterial activity against S. aureus. 23 Tang et al constructed a supramolecular hydrogel based on an amino acid-modied conjugated oligomer, which exhibited efficient capture and specic killing properties toward antibioticresistant bacteria. 24 Despite many efforts that have been devoted to developing functionalized supramolecular hydrogels, unfortunately, the ideal LMWH is usually not easy to obtain.…”

The Diverse World of Foldamers: Endless Possibilities of Self-Assembly

“…Additionally, oligomers built using exclusively non-standard α-amino acids, or a mixture of proteinogenic and non-proteinogenic α-residues, have been almost completely excluded from this review, albeit their interesting studies sometimes included the use of peculiar experimental techniques. For instance, this exclusion applies to α-peptides containing mainly α-aminoisobutyric acid (Aib), for which only a few illustrative examples have been reported here, [ 34 ] and chiral α-dialkyl α-amino acids (e.g., synthetic derivatives of naturally-occurring peptaibiotics and peptaibols [ 35 , 36 , 37 ]), whose self-assembly has been thoroughly studied [ 38 , 39 , 40 ], especially in the presence of phospholipid membranes [ 41 ], as shown in Figure 3 d, and to low-molecular-weight gelators (LMWGs) based on short α-peptide derivatives [ 42 , 43 , 44 ] or pseudopeptides [ 45 , 46 ], which do not fulfill the foldamer definition adopted here. In addition, oligomers made only of different pseudoproline units (L-pyroglutamic acid, L- p Glu, trans -4-carboxybenzyl-5-methyloxazolidin- 2-one, L- or D-Oxd, and (4 R )-(2-oxo-1,3-oxazolidin-4-yl)-acetic acid, D-Oxac), as shown in Figure 3 e, which are sometimes included in the field of foldamers, have been excluded here [ 47 ].…”