Randal H. Eckert

TL;DR: The STAMPs presented here are capable of eliminating S. mutans from multispecies biofilms without affecting closely related noncariogenic oral streptococci, indicating the potential of these molecules to be developed into “probiotic” antibiotics which could selectively eliminate pathogens while preserving the protective benefits of a healthy normal flora.

TL;DR: The successful creation of the first synthetic, target-specific antimicrobial peptide, G10KHc, is reported, via addition of a rationally designed Pseudomonas-specific targeting moiety (KH) to a generally killing peptide (novispirin G10).

TL;DR: This study showed targeted removal of human cariogenic Streptococcus mutans within an in vitro oral multispecies community using a high-efficacy antimicrobial peptide—C16G2—as well as drastic reconstruction of the microbial structure following treatment.

TL;DR: In this paper, in various embodiments chimeric moieties are provided comprising an antimicrobial peptide attached to a peptide targeting moiety that binds a bacterial strain or species, and the chimeric peptide is used to provide novel targeted antimicrobial compositions.

TL;DR: The data suggest that C16G2 has a mechanism of action similar to that of traditional AMPs and kills S. mutans through disruption of the cell membrane, allowing small molecules to leak out of thecell, which is followed by a loss of membrane potential and cell death.