Antimicrobial Peptide Analogs From Scorpions: Modifications and Structure-Activity

Abstract

The rapid development of multidrug-resistant pathogens against conventional antibiotics is a global public health problem. The irrational use of antibiotics has promoted therapeutic limitations against different infections, making research of new molecules that can be applied to treat infections necessary. Antimicrobial peptides (AMPs) are a class of promising antibiotic molecules as they present broad action spectrum, potent activity, and do not easily induce resistance. Several AMPs from scorpion venoms have been described as a potential source for the development of new drugs; however, some limitations to their application are also observed. Here, we describe strategies used in several approaches to optimize scorpion AMPs, addressing their primary sequence, biotechnological potential, and characteristics that should be considered when developing an AMP derived from scorpion venoms. In addition, this review may contribute towards improving the understanding of rationally designing new molecules, targeting functional AMPs that may have a therapeutic application.

Identification of an Antimicrobial Peptide from the Venom of the Trinidad Thick-Tailed Scorpion Tityus trinitatis with Potent Activity against ESKAPE Pathogens and Clostridioides difficile

“…Nevertheless, TtAP-1 represents a template for the design of analogs containing appropriate amino acid substitutions that preserve the high potencies against pathogenic microorganisms while at the same time reducing toxicities against mammalian cells and increasing their half-lives in circulation. Strategies for effecting such transformations in cationic, α- helical peptides such as TtAP-1 are well established and are the subject of recent reviews [ 55 , 56 , 57 ].…”

Short-Chained Linear Scorpion Peptides: A Pool for Novel Antimicrobials

“…The toroidal-pore model is also known as the wormhole model. Despite similarities to the barrel-stave model, an important difference is that the peptide helices insert into cell membranes and bind with the lipids, forming toroidal-pore complexes [32]. Several peptides such as magainin II and melittin as well as aurein have been shown to form toroidal pores [33].…”

Peptides as Therapeutic Agents: Challenges and Opportunities in the Green Transition Era

“…Accordingly, both peptide analogues and peptidomimetics have flourished over the past years and stand out for their own importance as a well-defined category of therapeutics; hence, their discussion is beyond the scope of the present work. For an in-depth discussion on this topic, several excellent publications can be found in the recent literature [14][15][16][17][18][19][20].…”