Peptide Library

Binds the viral gp41 protein while it is in the middle of fusing with a cell, locking it open so the virus cannot enter

In the presence of calcium it inserts its fatty tail into the bacterial cell membrane, forms clusters, and lets ions leak out, killing the cell quickly without lysing it

Cationic peptides that disrupt microbial membranes (partly via binding the cell-wall precursor lipid II) and also signal to the immune system, recruiting and activating immune cells

A detergent-like peptide that inserts into and lyses cell membranes — this is behind both its antimicrobial/anticancer activity in the lab and its toxicity and pain

Cationic peptides that bind and disrupt microbial membranes and sequester iron bacteria need; the parent protein also modulates immunity

Cationic membrane-disrupting peptide that permeabilises bacterial membranes, giving broad activity and a low tendency to select resistance

Cationic membrane-active peptide with antibacterial and antifungal activity, applied topically for skin and catheter-site indications

Binds lipid II (the bacterial cell-wall building block), both blocking wall synthesis and using lipid II as a docking point to punch pores in the membrane

Forms head-to-head dimer ion channels in the bacterial membrane that let Na⁺/K⁺ leak through, collapsing the ion gradients the cell needs

Their positive charge binds lipid A of lipopolysaccharide in the Gram-negative outer membrane, disrupting it and the inner membrane and killing the cell

Strongly cationic and amphipathic — bind anionic bacterial membranes and lipopolysaccharide, permeabilise the membrane and kill rapidly; the same physical chemistry makes them cytotoxic to mammalian cells and red cells at higher…

Non-competitively inhibit β-(1,3)-D-glucan synthase, an enzyme fungi need to build their cell wall and humans do not have, causing fungal cell lysis

Bind the D-alanyl-D-alanine end of peptidoglycan precursors, physically blocking the enzymes that build the bacterial cell wall; lipoglycopeptides additionally anchor to and disrupt the membrane