ArticleChembiochem : a European journal of chemical biology2026
Structure-Function Regulation of Proteolytically Stable Amphiphilic Peptide-Based Soft Materials With Antimicrobial Efficacy Against Drug-Resistant Strains and Anticancer Activity in Triple-Negative Breast Cancer Cells.
Article in Chembiochem : a European journal of chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The rapid progress of multidrug-resistant (MDR) bacterial infections and the clinical aggressiveness of triple-negative breast cancer (TNBC) possess a great problem to human beings. It necessitates the discovery and development of multifunctional therapeutic biomaterials. Herein, we report two enzymatically stable short cationic peptide hydrogelators comprising of N-terminal lysine headgroups, non-coded amino acid spacers, aromatic phenylalanine residues, and dodecylamine tails. These amphiphilic peptides are rapidly self-assembled in Tris-HCl buffer (pH 7.4) to form hydrogels with nanofibrillar network. Remarkably, both of these hydrogelators exhibit potent antibacterial activity against several Gram-positive and Gram-negative drug-resistant strains, functioning through multitiered mechanism including membrane permeabilization, trans-membrane depolarization, and intracellular reactive oxygen species (ROS) generation. Moreover, one of these peptide amphiphiles demonstrates a significant anticancer efficacy (with IC
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