Why to Study Peptides from Venomous and Poisonous Animals?

Oliveira, Ana; Soares, Andreimar M.; Silva, Saulo L. da

doi:10.1007/s10989-023-10543-0

Cited by 6 publications

(5 citation statements)

References 438 publications

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“…The exploration of alternative therapeutic options has led researchers to delve into the world of animal peptides [37][38][39]. Many creatures in the animal kingdom produce peptides as a part of their defense mechanisms, signaling systems, or for various physiological functions.…”

Section: Antinociceptive Peptides Of Animal Originmentioning

confidence: 99%

“…Animal peptides exhibit antinociceptive properties by interacting with the body's pain-signaling pathways. They can modulate pain perception through various mechanisms, including interaction with receptors involved in pain transmission, inhibition of inflammatory processes, and modulation of neuronal excitability [39]. Understanding the specific mechanisms through which animal peptides exert their antinociceptive effects is crucial for developing targeted and effective pain management strategies.…”

Section: Antinociceptive Peptides Of Animal Originmentioning

confidence: 99%

“…Several studies reported that peptide toxins purified from snake venom have the potential to become new painkillers [39].…”

Section: Peptides From Snake Venommentioning

confidence: 99%

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Analgesic Peptides: From Natural Diversity to Rational Design

Gach-Janczak,

Biernat,

Kuczer

et al. 2024

Molecules

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Pain affects one-third of the global population and is a significant public health issue. The use of opioid drugs, which are the strongest painkillers, is associated with several side effects, such as tolerance, addiction, overdose, and even death. An increasing demand for novel, safer analgesic agents is a driving force for exploring natural sources of bioactive peptides with antinociceptive activity. Since the G protein-coupled receptors (GPCRs) play a crucial role in pain modulation, the discovery of new peptide ligands for GPCRs is a significant challenge for novel drug development. The aim of this review is to present peptides of human and animal origin with antinociceptive potential and to show the possibilities of their modification, as well as the design of novel structures. The study presents the current knowledge on structure-activity relationship in the design of peptide-based biomimetic compounds, the modification strategies directed at increasing the antinociceptive activity, and improvement of metabolic stability and pharmacodynamic profile. The procedures employed in prolonged drug delivery of emerging compounds are also discussed. The work summarizes the conditions leading to the development of potential morphine replacements.

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Section: Antinociceptive Peptides Of Animal Originmentioning

confidence: 99%

Section: Antinociceptive Peptides Of Animal Originmentioning

confidence: 99%

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Analgesic Peptides: From Natural Diversity to Rational Design

Gach-Janczak,

Biernat,

Kuczer

et al. 2024

Molecules

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“…Scorpion venom has proved to be a rich source of biologically active peptides that may have therapeutic potential. These include compounds with antimicrobial, anti-tumor, anti-inflammatory, anti-angiogenic and analgesic properties, and peptides that may be developed into drugs for treatments of diseases associated with ion channels (reviewed in [ 1 ]). The genus Tityus , belonging to the extensive family Buthidae, comprises more than 200 species that are widely distributed in Central and South America.…”

Section: Introductionmentioning

confidence: 99%

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

Mechkarska,

Cunning,

Taggart

et al. 2023

Antibiotics

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Envenomation by the Trinidad thick-tailed scorpion Tityus trinitatis may result in fatal myocarditis and there is a high incidence of acute pancreatitis among survivors. Peptidomic analysis (reversed-phase HPLC followed by MALDI-TOF mass spectrometry and automated Edman degradation) of T. trinitatis venom led to the isolation and characterization of three peptides with antimicrobial activity. Their primary structures were established asTtAP-1 (FLGSLFSIGSKLLPGVFKLFSRKKQ.NH2), TtAP-2 (IFGMIPGLIGGLISAFK.NH2) and TtAP-3 (FFSLIPSLIGGLVSAIK.NH2). In addition, potassium channel and sodium channel toxins, present in the venom in high abundance, were identified by CID-MS/MS sequence analysis. TtAP-1 was the most potent against a range of clinically relevant Gram-positive and Gram-negative aerobes and against the anaerobe Clostridioides difficile (MIC = 3.1–12.5 µg/mL). At a concentration of 1× MIC, TtAP-1 produced rapid cell death (<15 min against Acinetobacter baumannii and Staphylococcus aureus). The therapeutic potential of TtAP-1 as an anti-infective agent is limited by its high hemolytic activity (LC50 = 18 µg/mL against mouse erythrocytes) but the peptide constitutes a template for the design of analogs that maintain the high bactericidal activity against ESKAPE pathogens but are less toxic to human cells. It is suggested that the antimicrobial peptides in the scorpion venom facilitate the action of the neurotoxins by increasing the membrane permeability of cells from either prey or predator.

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“…These molecules exhibit a wide range of biological activities, including antimicrobial, antifungal, antiparasitic, antibiofilm, and, in the last decade, anticancer properties [1][2][3]. Their broad biological activity has been associated with an interaction with several molecular targets, particularly cell membrane, enzymes, and transmembrane receptors [4]. BAPs have been identified from countless sources, like plants, mammals, insects, and, one of the most interesting sources, venoms.…”

Section: Introductionmentioning

confidence: 99%

Biophysical Insights into the Antitumoral Activity of Crotalicidin against Breast Cancer Model Membranes

Klaiss-Luna,

Giraldo-Lorza,

Jemioła-Rzemińska

et al. 2023

IJMS

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Bioactive peptides have emerged as promising therapeutic agents with antimicrobial, antifungal, antiparasitic, and, recently, antitumoral properties with a mechanism of action based on membrane destabilization and cell death, often involving a conformational change in the peptide. This biophysical study aims to provide preliminary insights into the membrane-level antitumoral mode of action of crotalicidin, a cationic host defense peptide from rattlesnake venom, toward breast cancer cell lines. The lipid composition of breast cancer cell lines was obtained after lipid extraction and quantification to prepare representative cell membrane models. Membrane–peptide interaction studies were performed using differential scanning calorimetry and Fourier-transform infrared spectroscopy. The outcome evidences the potential antitumoral activity and selectivity of crotalicidin toward breast cancer cell lines and suggests a mechanism initiated by the electrostatic interaction of the peptide with the lipid bilayer surface and posterior conformation change with membrane intercalation between the acyl chains in negatively charged lipid systems. This research provides valuable information that clears up the antitumoral mode of action of crotalicidin.

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Why to Study Peptides from Venomous and Poisonous Animals?

Cited by 6 publications

References 438 publications

Analgesic Peptides: From Natural Diversity to Rational Design

Analgesic Peptides: From Natural Diversity to Rational Design

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

Biophysical Insights into the Antitumoral Activity of Crotalicidin against Breast Cancer Model Membranes

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