Shanmugapriya Sothiselvam

TL;DR: An overview of the main physicochemical features that can be engineered to achieve enhanced bioactivity of antimicrobials is provided and current strategies being used to design AMPs are described.

TL;DR: It is shown that the antibiotic induces stalling, even without significant contacts with the peptide, by allosterically altering the peptidyl transferase center of the ribosome, unveils a previously unknown role of cofactors for translation arrest and demonstrates the existence of a functional link between the exit tunnel and the catalytic Center of the Ribosome.

TL;DR: It is shown that erythromycin resistance methyltransferase expression reduces cell fitness, which provides a plausible explanation why erm genes have evolved to be inducible and underscores the importance of nascent peptide recognition by the ribosome for generating a balanced cellular proteome.

TL;DR: In this paper, the structure of ribosomes arrested during the synthesis of an Arg-Leu-Arg sequence by the macrolide erythromycin and the ketolide telithromycin (TEL) was presented.

TL;DR: Using comprehensive mutational analysis and biochemical experiments with synthetic substrate analogs, it is found that the positive charge of these specific residues and the length of their side chains underlie inefficient peptide bond formation in the macrolide-bound ribosome.