Pseudonajide peptide derived from snake venom alters cell envelope integrity interfering on biofilm formation in Staphylococcus epidermidis

Abstract

Background: The increase in bacterial resistance phenotype cases is a global health problem. New strategies must be explored by the scientific community in order to create new treatment alternatives. Animal venoms are a good source for antimicrobial peptides (AMPs), which are excellent candidates for new antimicrobial drug development. Cathelicidin-related antimicrobial peptides (CRAMPs) from snake venoms have been studied as a model for the design of new antimicrobial pharmaceuticals against bacterial infections. Results: In this study we present an 11 amino acid-long peptide, named pseudonajide, which is derived from a Pseudonaja textilis venom peptide and has antimicrobial and antibiofilm activity against Staphylococcus epidermidis. Pseudonajide was selected based on the sequence alignments of various snake venom peptides that displayed activity against bacteria. Antibiofilm activity assays with pseudonajide concentrations ranging from 3.12 to 100 μM showed that the lowest concentration to inhibit biofilm formation was 25 μM. Microscopy analysis demonstrated that pseudonajide interacts with the bacterial cell envelope, disrupting the cell walls and membranes, leading to morphological defects in prokaryotes. Conclusions: Our results suggest that pseudonajide's positives charges interact with negatively charged cell wall components of S. epidermidis, leading to cell damage and inhibiting biofilm formation.

Combined Proteotranscriptomic-Based Strategy to Discover Novel Antimicrobial Peptides from Cone Snails

“…For example, the investigation of scorpion venoms led to the discovery of Hadrurin, Scorpine, Vejovine, StCT2, Pandinin 1, and Pandinin 2, which are effective antimicrobial peptides [ 19 , 20 , 21 , 22 , 23 ]. Similar studies also found antimicrobial peptides in snakes, spiders, bees, ants, centipedes, lugworms, wasps, and cuttlefish [ 15 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 ].…”

A Supramolecular Antidote to Macromolecular Toxins Prepared through Coassembly of Macrocyclic Amphiphiles

“…Next, we expanded the application scope of CCA‐CD as a supramolecular antidote to other macromolecular toxins as long as selective and strong binding is achieved. Considering latarcin 1 ( Figure a), a peptide from spider venom, [ 26 ] and crotalicidin (Figure 3b), a peptide from snake venom, [ 27 ] as examples, we studied the universality of CCA‐CD as a sequestration host for this type of macromolecular toxins displaying membrane‐damaging toxicity. The association constants were determined to be (3.03 ± 1.79) × 10 8 m −1 ( N = 2) for latarcin 1 (Figure 3c,d) and (5.42 ± 2.41) × 10 8 m −1 ( N = 3) for crotalicidin (Figure 3e,f), both of which were strong enough to ensure that CCA‐CD could effectively sequester them.…”

Disclosure of a Promising Lead to Tackle Complicated Skin and Skin Structure Infections: Antimicrobial and Antibiofilm Actions of Peptide PP4-3.1

“…Antimicrobial peptides or, in a broader sense, host defense peptides (HDP), are frontrunners in providing new alternatives to current antibiotics, which are becoming virtually useless against the growing menace of multidrug resistant pathogens. While recent research has unveiled very promising HDP from either natural sources [35][36][37] or recombinant technology [38,39], most of the HDP that have been advanced over the past few years as prospective relevant players in the combat against infectious diseases are of synthetic origin. Rational design, along with chemical synthesis, offers a multiplicity of peptide-based constructs with no match in Nature, enabling a fine tuning of their pharmacodynamic and pharmacokinetic properties, thereby improving their fitness to reach the clinics [40][41][42].…”