The partitioning of the wasp venom peptide mastoparan-X (MPX) into neutral and negatively
charged lipid membranes has been compared with two new synthetic analogs of MPX …

Many antimicrobial peptides undergo a coil-to-helix transition upon binding to membranes.
While this conformational transition is critical for function, little is known about the underlying …

The emergence of antibiotic-resistant clinical isolates and the decreased rate of
development of new antibiotics are a constant threat to human health. In this context, the …

The discovery of new anti-infective compounds is stagnating and multi-resistant bacteria
continue to emerge, threatening to end the “antibiotic era”. Antimicrobial peptides (AMPs) …

Abstract Mastoparan X (MPX: INWKGIAAMAKKLL-NH 2) belongs to a family of ionophoric
peptides found in wasp venom. Upon binding to the membrane, MPX increases the cell's …

Mastoparans are cationic peptides with multifunctional pharmacological properties.
Mastoparan‐R1 and mastoparan‐R4 were computationally designed based on native …

Many potent antimicrobial peptides also present hemolytic activity, an undesired collateral
effect for the therapeutic application. Unlike other mastoparan peptides, Polybia-MP1 …

Some mastoparan peptides extracted from social wasps display antimicrobial activity and
some are hemolytic and cytotoxic. Although the cell specificity of these peptides is complex …

Abstract Mastoparan B (MP-B) is an antimicrobial cationic tetradecapeptide amide isolated
from the venom of the hornet Vespa basalis. NMR spectroscopy was used to study the …

Antimicrobial peptides of the mastoparans family exert their bactericidal activity by binding to
lipid membranes, inducing pores or defects and leaking the internal contents of vesicles and …