Antimicrobial Activity Developed by Scorpion Venoms and Its Peptide Component

Abstract

Microbial infections represent a problem of great importance at the public health level, with a high rate of morbidity-mortality worldwide. However, treating the different diseases generated by microorganisms requires a gradual increase in acquired resistance when applying or using them against various antibiotic therapies. Resistance is caused by various molecular mechanisms of microorganisms, thus reducing their effectiveness. Consequently, there is a need to search for new opportunities through natural sources with antimicrobial activity. One alternative is using peptides present in different scorpion venoms, specifically from the Buthidae family. Different peptides with biological activity in microorganisms have been characterized as preventing their growth or inhibiting their replication. Therefore, they represent an alternative to be used in the design and development of new-generation antimicrobial drugs in different types of microorganisms, such as bacteria, fungi, viruses, and parasites. Essential aspects for its disclosure, as shown in this review, are the studies carried out on different types of peptides in scorpion venoms with activity against pathogenic microorganisms, highlighting their high therapeutic potential.

Profiling the Linear Peptides of Venom from the Brazilian Scorpion Tityus serrulatus: Structural and Functional Characterization

“…The small linear peptide toxins usually cause cytolysis, inflammation, pain, edema formation, and disturbance of movements. Scorpions usually paralyze prey (using neurotoxins) to be eaten later; in the meantime it is necessary to prevent the infection of these prey by bacteria, requiring the production of antibiotic peptides in the venom . For evaluating these actions, 12 peptides were synthesized using the solid-phase strategy.…”

“…peptides in the venom. 23 For evaluating these actions, 12 peptides were synthesized using the solid-phase strategy. Synthetic peptides were submitted to bioassays of hemolysis, mast cell degranulation, lactate dehydrogenase (LDH) release from mast cells, edema formation in mice hind paws, nociception, rearing, locomotion in an observation arena, and antibiosis.…”

Exploring the Therapeutic Potential of Scorpion-Derived Css54 Peptide Against Candida albicans

“…To address antifungal resistance, new antifungal agents have been developed using AMPs isolated from a wide variety of organisms to overcome this issue. The mode of action of AMPs involves membrane disruption and targeting of intracellular components, inhibiting essential microbial metabolic functions, and thus showing minimal correlation with antimicrobial resistance (Rincón-Cortés et al, 2022 ).…”

Cationicity Enhancement on the Hydrophilic Face of Ctriporin Significantly Reduces Its Hemolytic Activity and Improves the Antimicrobial Activity against Antibiotic-Resistant ESKAPE Pathogens

“…Cationic α-helical antimicrobial peptides (CαAMPs) have been largely identified from a wide range of organisms and reported to possess bactericidal activity against different kinds of pathogens [ 4 , 5 , 6 , 7 , 8 , 9 ]. CαAMPs are cationic amphiphilic molecules with a distinct hydrophilic face on which polar residues often position and a hydrophobic face where nonpolar residues often gather.…”

“…A wealth of CαAMPs have been identified from the venom glands of various scorpion species [ 4 , 9 , 15 , 16 ]. Among these peptides, the members of short cationic AMP family are a group of cationic α-helical peptides with 17 to 19 residues, including Ctriporin [ 17 ], Mucroporin [ 18 ], Imcroporin [ 19 ], Stigmurin [ 20 ], TsAP-1 and TsAP-2 [ 21 ], AamAP1 and AamAP2 [ 22 ], and BmKb1 and BmKb2 [ 23 ].…”