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From Animal Venoms to Solutions: In Honor of Professor Lourival...
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From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Animal Venoms".

Deadline for manuscript submissions: 15 February 2025 | Viewed by 16237

Special Issue Editor

Prof. Dr. Elisabeth Ferroni Schwartz

E-Mail Website
Guest Editor
Department of Physiological Sciences, Institute of Biological Sciences, University of Brasilia, Brasilia 70910-900, DF, Brazil
Interests: ion channel; scorpion venom; theraphosidae venom; neurotoxins
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

It has not been precisely determined when humans started to use animal venoms for medicinal purposes. Thousands of years ago, animal venoms were the basis of preparations used as treatments for smallpox, leprosy, fever and wound healing. In the 1st century AD, a mixture named theriac, or theriaca, which contained leaven, honey and the flesh of venomous animals, including that of scorpions and viper snakes, was developed by Greeks and used by Romans, as well as in Persia, China and India. Historical data indicate that even the Roman emperor Marcus Aurelius took it on a regular basis. Theriac was used until the 18th century.

The history of the prospection of venom compounds also traces back more than two millennia.

Venom glands, injection apparatus and noxious secretions have evolved in animals for the capture of prey and for defense purposes. Venomous vertebrates and invertebrates possess exocrine cells or glands that produce energetically expensive, highly efficient and complex mixtures, whose compositions depend on the venomous species. Snakes, spiders, scorpions, bees, wasps, anemones, cone snails and jellyfishes are the most commonly studied venomous animals.

Mainly due to its medical significance, many studies comprise the effects of whole venom, the mechanism of action of the main toxins and the search for specific human envenoming treatment. Bites or stings by certain venomous species result in severe envenomation and high mortality rates. The most effective treatment to date is the use of injectable antivenoms.

Besides the health-related importance regarding human envenoming, venom-related research relating to the search for new compounds that are potential templates for the development of new pharmacological tools and medicines has been growing fast in recent decades. For instance, the long evolution process, the distribution to almost all environments and the diversity of prey and predators resulted in very complex venoms that contain molecules with unique biological properties, which can be used in both basic science and clinical applications.

Over the past five decades, many researchers have studied animal venoms. Prof. Lourival D Possani deserves to be highlighted for his broad contributions in the area, particularly his significant contributions to the completion of the first original works that describe scorpion toxins as modifiers of the function of different ion channels and for the discovery of two new antibiotics. During the period 1971–1973, he completed a postdoctoral stay in the laboratory of Dr. Edward Reich at Rockefeller University, NY, USA, where he worked with components of animal venoms and participated in the isolation of the acetylcholine receptor. In 1974, he began his academic career in Mexico at the Institute of Biology of the UNAM, working on aspects related to the functioning of GABAergic neurons in the group of Dr. Ricardo Tapia. Shortly after, he recognized that Mexico had a public health problem regarding scorpion stings and that the molecular identities of the components of their venoms and their molecular mechanism of action were unknown. Thus, Prof. Possani formed his research group with the objective of characterizing the components of scorpion venoms. In 2024, he will turn 85 years old, and Toxins has decided to pay tribute with a special edition.

The Toxins Special Issue entitled “From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday” intends to amalgamate high-quality, original, basic and clinical research articles by established academic authors as well as new researchers. Articles reporting research data obtained in the field of animal venom and covering a wide range of topics including human envenoming, antivenoms, venom compounds, their mechanism of action and the prospection of new drugs from animal venoms will be published.

Prof. Dr. Elisabeth Ferroni Schwartz
Guest Editor

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Keywords

  • venom
  • snake
  • spider
  • scorpion
  • toxins
  • antivenom
  • venom prospection
  • anemone
  • conus
  • ant
  • bee
  • wasp
  • jellyfish
  • stingrays
  • lonomia
  • tarantula
  • viper

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Published Papers (9 papers)

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Research

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14 pages, 6441 KiB  
Article
Cardiotoxic Effects of Lachesis acrochorda Snake Venom in Anesthetized Wistar Rats
by Karen Leonor Ángel-Camilo, Mary Luz Bueno-Ospina, Ivonne Carolina Bolaños Burgos, Santiago Ayerbe-González, José Beltrán-Vidal, Ana Acosta, Jaime Álvarez-Soler and Jimmy Alexander Guerrero-Vargas
Toxins 2024, 16(9), 377; https://doi.org/10.3390/toxins16090377 - 28 Aug 2024
Viewed by 1380
Abstract
Ophidism is a public health problem in tropical countries, occurring predominantly in rural areas. In Colombia, among the species responsible for snakebite envenomation, inflicting high mortality, is the Chocoan bushmaster, Lachesis acrochorda, better known locally by the names “verrugosa (warty)” and [...] Read more.
Ophidism is a public health problem in tropical countries, occurring predominantly in rural areas. In Colombia, among the species responsible for snakebite envenomation, inflicting high mortality, is the Chocoan bushmaster, Lachesis acrochorda, better known locally by the names “verrugosa (warty)” and “pudridora (rot-causing)”. In this research, the cardiotoxic effect of the venom of L. acrochorda in male Wistar rats weighing 230 ± 20 g was evaluated. A statistical design of randomized blocks was implemented with three treated groups, injected with lyophilized venom (doses of 3.22 μg/g, 6.43 μg/g, 12.86 μg/g), and a control group injected with 0.9% saline solution. Electrocardiographic (ECG) recordings were taken from the anesthetized animals, revealing an increase in the amplitude of the P and T waves and an increase in the duration of the QT intervals in the electrocardiographic recordings. These increases were not observed in the control biomodels. In the analysis of the CK and CK-MB enzyme levels, increases were also observed in the levels of cardiac isoenzymes in the injected animals, but none in the control animals. The histopathological analyses carried out reveal that the injected animals showed effects such as interfibrillar and perivascular edema, cellular shortening of the cardiomyocytes, foci with tissue destructuring, and necrosis with contraction bands. In conclusion, the venom of the Lachesis acrochorda snake increases the P and T waves and the QT interval and increases the CK and CK-MB enzymes in the blood. Additionally, it causes interfibrillar and perivascular edema in the cardiac tissue, cardiocytolysis, and contraction bands. Full article
(This article belongs to the Special Issue From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday)
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19 pages, 3710 KiB  
Article
Nanofractionation Analytics for Comparing MALDI-MS and ESI-MS Data of Viperidae Snake Venom Toxins
by Haifeng Xu, Jesse Mastenbroek, Natascha T. B. Krikke, Susan El-Asal, Rama Mutlaq, Nicholas R. Casewell, Julien Slagboom and Jeroen Kool
Toxins 2024, 16(8), 370; https://doi.org/10.3390/toxins16080370 - 21 Aug 2024
Cited by 1 | Viewed by 1369
Abstract
Worldwide, it is estimated that there are 1.8 to 2.7 million cases of envenoming caused by snakebites. Snake venom is a complex mixture of protein toxins, lipids, small molecules, and salts, with the proteins typically responsible for causing pathology in snakebite victims. For [...] Read more.
Worldwide, it is estimated that there are 1.8 to 2.7 million cases of envenoming caused by snakebites. Snake venom is a complex mixture of protein toxins, lipids, small molecules, and salts, with the proteins typically responsible for causing pathology in snakebite victims. For their chemical characterization and identification, analytical methods are required. Reversed-phase liquid chromatography coupled with electrospray ionization mass spectrometry (RP-LC-ESI-MS) is a widely used technique due to its ease of use, sensitivity, and ability to be directly coupled after LC separation. This method allows for the efficient separation of complex mixtures and sensitive detection of analytes. On the other hand, matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) is also sometimes used, and though it typically requires additional sample preparation steps, it offers desirable suitability for the analysis of larger biomolecules. In this study, seven medically important viperid snake venoms were separated into their respective venom toxins and measured by ESI-MS. In parallel, using nanofractionation analytics, post-column high-resolution fractionation was used to collect the eluting toxins for further processing for MALDI-MS analysis. Our comparative results showed that the deconvoluted snake venom toxin masses were observed with good sensitivity from both ESI-MS and MALDI-MS approaches and presented overlap in the toxin masses recovered (between 25% and 57%, depending on the venom analyzed). The mass range of the toxins detected in high abundance was between 4 and 28 kDa. In total, 39 masses were found in both the ESI-MS and/or MALDI-MS analyses, with most being between 5 and 9 kDa (46%), 13 and 15 kDa (38%), and 24 and 28 kDa (13%) in size. Next to the post-column MS analyses, additional coagulation bioassaying was performed to demonstrate the parallel post-column assessment of venom activity in the workflow. Most nanofractionated venoms exhibited anticoagulant activity, with three venoms additionally exhibiting toxins with clear procoagulant activity (Bothrops asper, Crotalus atrox, and Daboia russelii) observed post-column. The results of this study highlight the complementarity of ESI-MS and MALDI-MS approaches for characterizing snake venom toxins and provide a complementary overview of defined toxin masses found in a diversity of viper snake venoms. Full article
(This article belongs to the Special Issue From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday)
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11 pages, 3032 KiB  
Article
Evaluating a Venom-Bioinspired Peptide, NOR-1202, as an Antiepileptic Treatment in Male Mice Models
by Maria Varela Torres Quintanilha, Giovanna de Azevedo Mello Gobbo, Gabriela Beserra Pinheiro, Adolfo Carlos Barros de Souza, Luana Cristina Camargo and Marcia Renata Mortari
Toxins 2024, 16(8), 342; https://doi.org/10.3390/toxins16080342 - 5 Aug 2024
Cited by 1 | Viewed by 1125
Abstract
Epilepsy, a neurological disorder characterized by excessive neuronal activity and synchronized electrical discharges, ranks among the most prevalent global neurological conditions. Despite common use, antiepileptic drugs often result in adverse effects and lack effectiveness in controlling seizures in temporal lobe epilepsy (TLE) patients. [...] Read more.
Epilepsy, a neurological disorder characterized by excessive neuronal activity and synchronized electrical discharges, ranks among the most prevalent global neurological conditions. Despite common use, antiepileptic drugs often result in adverse effects and lack effectiveness in controlling seizures in temporal lobe epilepsy (TLE) patients. Recent research explored the potential of occidentalin-1202, a peptide inspired by Polybia occidentalis venom, in safeguarding Wistar rats from chemically induced seizures. The present study evaluated the new analog from occidentalin-1202 named NOR-1202 using acute and chronic pilocarpine-induced models and an acute kainic acid (KA) male mice model. NOR-1202 was administered through the intracerebroventricular (i.c.v.), subcutaneous, or intraperitoneal routes, with stereotaxic procedures for the i.c.v. injection. In the acute pilocarpine-induced model, NOR-1202 (i.c.v.) protected against generalized seizures and mortality but lacked systemic antiepileptic activity. In the KA model, it did not prevent generalized seizures but improved survival. In the chronic TLE model, NOR-1202′s ED50 did not differ significantly from the epileptic or healthy groups regarding time spent in spontaneous recurrent seizures during the five-day treatment. However, the NOR-1202 group exhibited more seizures than the healthy group on the second day of treatment. In summary, NOR-1202 exhibits antiepileptic effects against chemoconvulsant-induced seizures, but no effect was observed when administered systemically. Full article
(This article belongs to the Special Issue From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday)
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15 pages, 2994 KiB  
Article
Venomics of Scorpion Ananteris platnicki (Lourenço, 1993), a New World Buthid That Inhabits Costa Rica and Panama
by Cecilia Díaz, Bruno Lomonte, Arturo Chang-Castillo, Fabián Bonilla, Adriana Alfaro-Chinchilla, Felipe Triana, Diego Angulo, Julián Fernández and Mahmood Sasa
Toxins 2024, 16(8), 327; https://doi.org/10.3390/toxins16080327 - 23 Jul 2024
Viewed by 1285
Abstract
Ananteris is a scorpion genus that inhabits dry and seasonal areas of South and Central America. It is located in a distinctive morpho-group of Buthids, the ‘Ananteris group’, which also includes species distributed in the Old World. Because of the lack of [...] Read more.
Ananteris is a scorpion genus that inhabits dry and seasonal areas of South and Central America. It is located in a distinctive morpho-group of Buthids, the ‘Ananteris group’, which also includes species distributed in the Old World. Because of the lack of information on venom composition, the study of Ananteris species could have biological and medical relevance. We conducted a venomics analysis of Ananteris platnicki, a tiny scorpion that inhabits Panama and Costa Rica, which shows the presence of putative toxins targeting ion channels, as well as proteins with similarity to hyaluronidases, proteinases, phospholipases A2, members of the CAP-domain family, and hemocyanins, among others. Venom proteolytic and hyaluronidase activities were corroborated. The determination of the primary sequences carried out by mass spectrometry evidences that several peptides are similar to the toxins present in venoms from Old World scorpion genera such as Mesobuthus, Lychas, and Isometrus, but others present in Tityus and Centruroides toxins. Even when this venom displays the characteristic protein families found in all Buthids, with a predominance of putative Na+-channel toxins and proteinases, some identified partial sequences are not common in venoms of the New World species, suggesting its differentiation into a distinctive group separated from other Buthids. Full article
(This article belongs to the Special Issue From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday)
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19 pages, 3821 KiB  
Article
Unveiling Tst3, a Multi-Target Gating Modifier Scorpion α Toxin from Tityus stigmurus Venom of Northeast Brazil: Evaluation and Comparison with Well-Studied Ts3 Toxin of Tityus serrulatus
by Diogo Vieira Tibery, João Antonio Alves Nunes, Daniel Oliveira da Mata, Luis Felipe Santos Menezes, Adolfo Carlos Barros de Souza, Matheus de Freitas Fernandes-Pedrosa, Werner Treptow and Elisabeth Ferroni Schwartz
Toxins 2024, 16(6), 257; https://doi.org/10.3390/toxins16060257 - 3 Jun 2024
Viewed by 1518
Abstract
Studies on the interaction sites of peptide toxins and ion channels typically involve site-directed mutations in toxins. However, natural mutant toxins exist among them, offering insights into how the evolutionary process has conserved crucial sequences for activities and molecular target selection. In this [...] Read more.
Studies on the interaction sites of peptide toxins and ion channels typically involve site-directed mutations in toxins. However, natural mutant toxins exist among them, offering insights into how the evolutionary process has conserved crucial sequences for activities and molecular target selection. In this study, we present a comparative investigation using electrophysiological approaches and computational analysis between two alpha toxins from evolutionarily close scorpion species of the genus Tityus, namely, Tst3 and Ts3 from T. stigmurus and T. serrulatus, respectively. These toxins exhibit three natural substitutions near the C-terminal region, which is directly involved in the interaction between alpha toxins and Nav channels. Additionally, we characterized the activity of the Tst3 toxin on Nav1.1-Nav1.7 channels. The three natural changes between the toxins did not alter sensitivity to Nav1.4, maintaining similar intensities regarding their ability to alter opening probabilities, delay fast inactivation, and induce persistent currents. Computational analysis demonstrated a preference for the down conformation of VSD4 and a shift in the conformational equilibrium towards this state. This illustrates that the sequence of these toxins retained the necessary information, even with alterations in the interaction site region. Through electrophysiological and computational analyses, screening of the Tst3 toxin on sodium isoform revealed its classification as a classic α-NaTx with a broad spectrum of activity. It effectively delays fast inactivation across all tested isoforms. Structural analysis of molecular energetics at the interface of the VSD4-Tst3 complex further confirmed this effect. Full article
(This article belongs to the Special Issue From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday)
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14 pages, 8459 KiB  
Article
Characterization of Sodium Channel Peptides Obtained from the Venom of the Scorpion Centruroides bonito
by Rita Restano-Cassulini, Timoteo Olamendi-Portugal, Lidia Riaño-Umbarila, Fernando Z. Zamudio, Gustavo Delgado-Prudencio, Baltazar Becerril and Lourival D. Possani
Toxins 2024, 16(3), 125; https://doi.org/10.3390/toxins16030125 - 1 Mar 2024
Cited by 2 | Viewed by 1992
Abstract
Five peptides were isolated from the venom of the Mexican scorpion Centruroides bonito by chromatographic procedures (molecular weight sieving, ion exchange columns, and HPLC) and were denoted Cbo1 to Cbo5. The first four peptides contain 66 amino acid residues and the last one [...] Read more.
Five peptides were isolated from the venom of the Mexican scorpion Centruroides bonito by chromatographic procedures (molecular weight sieving, ion exchange columns, and HPLC) and were denoted Cbo1 to Cbo5. The first four peptides contain 66 amino acid residues and the last one contains 65 amino acids, stabilized by four disulfide bonds, with a molecular weight spanning from about 7.5 to 7.8 kDa. Four of them are toxic to mice, and their function on human Na+ channels expressed in HEK and CHO cells was verified. One of them (Cbo5) did not show any physiological effects. The ones toxic to mice showed that they are modifiers of the gating mechanism of the channels and belong to the beta type scorpion toxin (β-ScTx), affecting mainly the Nav1.6 channels. A phylogenetic tree analysis of their sequences confirmed the high degree of amino acid similarities with other known bona fide β-ScTx. The envenomation caused by this venom in mice is treated by using commercially horse antivenom available in Mexico. The potential neutralization of the toxic components was evaluated by means of surface plasmon resonance using four antibody fragments (10FG2, HV, LR, and 11F) which have been developed by our group. These antitoxins are antibody fragments of single-chain antibody type, expressed in E. coli and capable of recognizing Cbo1 to Cbo4 toxins to various degrees. Full article
(This article belongs to the Special Issue From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday)
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Review

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15 pages, 1381 KiB  
Review
Therapeutic Potential of Bee and Wasp Venom in Anti-Arthritic Treatment: A Review
by Hongmei Sun, Yunxia Qu, Xiaojing Lei, Qingzhu Xu, Siming Li, Zhengmei Shi, Huai Xiao, Chenggui Zhang and Zhibin Yang
Toxins 2024, 16(11), 452; https://doi.org/10.3390/toxins16110452 - 22 Oct 2024
Viewed by 2572
Abstract
Arthritis has a high global prevalence. During the early ancient human era, bee (Apis) venom therapy was employed in Egypt, Greece, and China to alleviate ailments such as arthritis and neuralgia. In addition, bee venom has long been used as a [...] Read more.
Arthritis has a high global prevalence. During the early ancient human era, bee (Apis) venom therapy was employed in Egypt, Greece, and China to alleviate ailments such as arthritis and neuralgia. In addition, bee venom has long been used as a traditional medicine for immune-related diseases in Korea. Wasp (Vespa) venom is a folk medicine of the Jingpo people in Yunnan, China, and has been widely used to treat rheumatoid arthritis. In spite of this, the underlying mechanisms of bee and wasp venoms for the treatment of arthritis are yet to be fully understood. In recent years, researchers have investigated the potential anti-arthritic properties of bee and wasp venoms. Studies have shown that both bee and wasp venom can improve swelling, pain, and inflammation caused by arthritis. The difference is that bee venom reduces arthritis damage to bone and cartilage by inhibiting the IRAK2/TAK1/NF-κB signaling pathway, NF-κB signaling pathway, and JAK/STAT signaling pathway, as well as decreasing osteoclastogenesis by inhibiting the RANKL/RANK signaling pathway. Wasp venom, on the other hand, regulates synovial cell apoptosis via the Bax/Bcl-2 signaling pathway, inhibits the JAK/STAT signaling pathway to reduce inflammation production, and also ameliorates joint inflammation by regulating redox balance and iron death in synovial cells. This review provides a detailed overview of the various types of arthritis and their current therapeutic approaches; additionally, it comprehensively analyzes the therapeutic properties of bee venom, wasp venom, or venom components used as anti-arthritic drugs and explores their mechanisms of action in anti-arthritic therapy. Full article
(This article belongs to the Special Issue From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday)
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38 pages, 7473 KiB  
Review
Exploring the Diversity and Function of Serine Proteases in Toxicofera Reptile Venoms: A Comprehensive Overview
by Julia F. D. Vidal, Matheus F. Schwartz, Aisel V. Garay, Napoleão F. Valadares, Renata V. Bueno, Ana Carolina L. Monteiro, Sônia Maria de Freitas and João Alexandre R. G. Barbosa
Toxins 2024, 16(10), 428; https://doi.org/10.3390/toxins16100428 - 3 Oct 2024
Viewed by 1944
Abstract
Toxicofera reptile venoms are composed of several toxins, including serine proteases. These proteases are glycosylated enzymes that affect the prey’s hemostatic system. Their actions extend across the coagulation cascade, the kallikrein–kinin system, and platelet activation. Despite their specificity for different substrates, these enzymes [...] Read more.
Toxicofera reptile venoms are composed of several toxins, including serine proteases. These proteases are glycosylated enzymes that affect the prey’s hemostatic system. Their actions extend across the coagulation cascade, the kallikrein–kinin system, and platelet activation. Despite their specificity for different substrates, these enzymes are homologous across all toxicoferans and display high sequence similarity. The aim of this review is to compile decades of knowledge about venom serine proteases, showing the diversity of biochemically and biophysically characterized enzymes, their structural characteristics, advances in understanding their origin and evolution, as well as methods of obtaining enzymes and their biotechnological applications. Full article
(This article belongs to the Special Issue From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday)
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22 pages, 2744 KiB  
Review
Shining a Light on Venom-Peptide Receptors: Venom Peptides as Targeted Agents for In Vivo Molecular Imaging
by Chun Yuen Chow and Glenn F. King
Toxins 2024, 16(7), 307; https://doi.org/10.3390/toxins16070307 - 4 Jul 2024
Cited by 1 | Viewed by 2038
Abstract
Molecular imaging has revolutionised the field of biomedical research by providing a non-invasive means to visualise and understand biochemical processes within living organisms. Optical fluorescent imaging in particular allows researchers to gain valuable insights into the dynamic behaviour of a target of interest [...] Read more.
Molecular imaging has revolutionised the field of biomedical research by providing a non-invasive means to visualise and understand biochemical processes within living organisms. Optical fluorescent imaging in particular allows researchers to gain valuable insights into the dynamic behaviour of a target of interest in real time. Ion channels play a fundamental role in cellular signalling, and they are implicated in diverse pathological conditions, making them an attractive target in the field of molecular imaging. Many venom peptides exhibit exquisite selectivity and potency towards ion channels, rendering them ideal agents for molecular imaging applications. In this review, we illustrate the use of fluorescently-labelled venom peptides for disease diagnostics and intraoperative imaging of brain tumours and peripheral nerves. Finally, we address challenges for the development and clinical translation of venom peptides as nerve-targeted imaging agents. Full article
(This article belongs to the Special Issue From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday)
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