Multimeric TAT peptides are effective in vitro inhibitors of Staphylococcus saprophyticus

Abstract

TAT (48-60) is a tridecapeptide from the envelope protein of HIV that was previously shown to possess cell-penetrating properties and antibacterial activity, making it a potential drug delivery agent for anticancer drugs and as antibacterial compound. Previous reports indicated that dimerization enhances the desired bioactivity of TAT; hence, we sought to synthesize multimeric TAT peptides. Herein, we describe the effects of multimerization on the antibacterial activity and secondary structure of the peptide. Terminal modifications such as N-acetylation and C-amidation were employed in the design. TATp monomer, dimer, and tetramer were synthesized using solid-phase peptide synthesis, purified by reversed-phase HPLC, and then charac

Protein Transduction System Based on Tryptophan-zipper against Intracellular Infections via Inhibiting Ferroptosis of Macrophages

“…Interestingly, the TAT derived from human immunodeficiency virus (HIV) has been widely employed in the construction of cellular internalization materials, including lipid nanoparticles that penetrate the blood–brain barrier and click chemistry to link camptothecin, for fighting cancer . In addition, TAT, with its high surface positive charges, can localize bacterial membranes on a large scale and provide noncovalent forces to capture bacteria, thus forming amphiphilic materials distinct from antibiotics for sterilization. , Therefore, pathogenic microorganism affinity motifs based on the highly positively charged TATs are regarded as biomaterials with superior properties. Our group previously demonstrated that Tryptophan (Trp)-zipper-based antimicrobial motifs could form self-assembled micelles through cationic−π bonds and aromatic stacking with aromatic rings and, by virtue of this, possess robust antimicrobial capabilities .…”