Snake Venom Cathelicidins as Natural Antimicrobial Peptides.

Elizângela De Barros,Octávio L Franco,Nuno C Santos,Marlon H Cardoso,Regina M Gonçalves,Elizabete S Cândido

doi:10.3389/fphar.2019.01415

Abstract

Bioactive small molecules isolated from animals, plants, fungi and bacteria, including natural antimicrobial peptides, have shown great therapeutic potential worldwide. Among these peptides, snake venom cathelicidins are being widely exploited, because the variation in the composition of the venom reflects a range of biological activities that may be of biotechnological interest. Cathelicidins are short, cationic, and amphipathic molecules. They play an important role in host defense against microbial infections. We are currently facing a strong limitation on pharmacological interventions for infection control, which has become increasingly complex due to the lack of effective therapeutic options. In this review, we will focus on natural snake venom cathelicidins as promising candidates for the development of new antibacterial agents to fight antibiotic-resistant bacteria. We will highlight their antibacterial and antibiofilm activities, mechanism of action, and modulation of the innate immune response.

Highlights

The rapid increase in microbial resistance to different drugs has been raising concerns worldwide, encouraging the search for effective alternative treatments (Nathan and Cars, 2014), especially when dealing with multidrug-resistant pathogens (Koo and Seo, 2019)
This review provides information on snake venom antimicrobial peptides (AMPs), including their characterization, biological activities, modes of action, and structural profile
Due to this helix-breaker residue, NA-CATH has shown weaker helical circular dichroism (CD) signatures than other cathelicidin-like peptides designed based on the 11-residue pattern (KR(F/A)KKFFKK(L/P)K), which is derived from the natural NA-CATH. These studies have correlated the higher helical propensity of NACATH short analogs to their higher antibacterial and antibiofilm activities, when compared to the natural NA-CATH (Dean et al, 2011). These data, along with those for cathelicidin-BF, raise the question of whether the a-helical extension in the natural peptides would lead to improved antimicrobial potential or not, shedding some light on the role of C-terminal flexibility in these natural cathelicidinrelated antimicrobial peptides (CRAMPs)

Summary

Introduction

The rapid increase in microbial resistance to different drugs has been raising concerns worldwide, encouraging the search for effective alternative treatments (Nathan and Cars, 2014), especially when dealing with multidrug-resistant pathogens (Koo and Seo, 2019). In the same year, Wang et al (2008) reported the antimicrobial activity of cathelicidin-BF against 40 standard strains and clinical isolates, including multidrug-resistant strains of microorganisms, compared to antibiotics for therapeutic use.

Results

Conclusion