The Chemistry of Snake Venom and Its Medicinal Potential

Overview

Journal Nat Rev Chem

Publisher Springer Nature

Specialty Chemistry

Date 2022 Jun 15

PMID 35702592

Authors

Ana L Oliveira

Matilde F Viegas

Saulo L da Silva

Andreimar M Soares

Maria J Ramos

Pedro A Fernandes

Affiliations

Soon will be listed here.

Abstract

The fascination and fear of snakes dates back to time immemorial, with the first scientific treatise on snakebite envenoming, the Brooklyn Medical Papyrus, dating from ancient Egypt. Owing to their lethality, snakes have often been associated with images of perfidy, treachery and death. However, snakes did not always have such negative connotations. The curative capacity of venom has been known since antiquity, also making the snake a symbol of pharmacy and medicine. Today, there is renewed interest in pursuing snake-venom-based therapies. This Review focuses on the chemistry of snake venom and the potential for venom to be exploited for medicinal purposes in the development of drugs. The mixture of toxins that constitute snake venom is examined, focusing on the molecular structure, chemical reactivity and target recognition of the most bioactive toxins, from which bioactive drugs might be developed. The design and working mechanisms of snake-venom-derived drugs are illustrated, and the strategies by which toxins are transformed into therapeutics are analysed. Finally, the challenges in realizing the immense curative potential of snake venom are discussed, and chemical strategies by which a plethora of new drugs could be derived from snake venom are proposed.

Citing Articles

seed proteins effect on snake venom enzymes with antioxidant and antibacterial activities.

Tahir W, Fatima S, Moin S, Moin M, Waheed H J Taibah Univ Med Sci. 2025; 20(1):81-88.

PMID: 40034741 PMC: 11875155. DOI: 10.1016/j.jtumed.2025.01.005.

Emerging Trends in Snake Venom-Loaded Nanobiosystems for Advanced Medical Applications: A Comprehensive Overview.

Alves A, Barros A, Silva L, Carvalho L, Pereira G, Uchoa A Pharmaceutics. 2025; 17(2).

PMID: 40006571 PMC: 11858983. DOI: 10.3390/pharmaceutics17020204.

Antischistosomal Potential of Animal-Derived Natural Products and Compounds.

Fischer-Carvalho A, Taveira-Barbosa T, Verjovski-Almeida S, Haeberlein S, Sena Amaral M Microorganisms. 2025; 13(2).

PMID: 40005763 PMC: 11858059. DOI: 10.3390/microorganisms13020397.

The Versatility of Serine Proteases from Brazilian Venom: Their Roles in Snakebites and Drug Discovery.

Romanazzi M, Filardi E, Pires G, Cerveja M, Melo-Dos-Santos G, Oliveira I Biomolecules. 2025; 15(2).

PMID: 40001458 PMC: 11852464. DOI: 10.3390/biom15020154.

Insights into the Role of Proteolytic and Adhesive Domains of Snake Venom Metalloproteinases from spp. in the Control of Infection.

Teixeira S, Fernandes T, de Souza G, Luz L, Paschoalino M, Junior J Toxins (Basel). 2025; 17(2).

PMID: 39998112 PMC: 11861417. DOI: 10.3390/toxins17020095.

References

Park J, Do B, Lee J, Yang H, Nguyen A, Krupa M . Antinociceptive and Anti-Inflammatory Effects of Recombinant Crotamine in Mouse Models of Pain. Toxins (Basel). 2021; 13(10). PMC: 8538437. DOI: 10.3390/toxins13100707. View

Ferreira S, Greene L, Alabaster V, Bakhle Y, Vane J . Activity of various fractions of bradykinin potentiating factor against angiotensin I converting enzyme. Nature. 1970; 225(5230):379-80. DOI: 10.1038/225379a0. View

Tan K, Bay B, Gopalakrishnakone P . L-amino acid oxidase from snake venom and its anticancer potential. Toxicon. 2018; 144:7-13. DOI: 10.1016/j.toxicon.2018.01.015. View

Gutierrez J, Calvete J, Habib A, Harrison R, Williams D, Warrell D . Snakebite envenoming. Nat Rev Dis Primers. 2017; 3:17063. DOI: 10.1038/nrdp.2017.63. View

King G . Venoms as a platform for human drugs: translating toxins into therapeutics. Expert Opin Biol Ther. 2011; 11(11):1469-84. DOI: 10.1517/14712598.2011.621940. View

Olaoba O, Santos P, Selistre-de-Araujo H, de Souza D . Snake Venom Metalloproteinases (SVMPs): A structure-function update. Toxicon X. 2020; 7:100052. PMC: 7399193. DOI: 10.1016/j.toxcx.2020.100052. View

Warkentin T, Greinacher A, Koster A . Bivalirudin. Thromb Haemost. 2008; 99(5):830-9. DOI: 10.1160/TH07-10-0644. View

Berg O, Gelb M, Tsai M, Jain M . Interfacial enzymology: the secreted phospholipase A(2)-paradigm. Chem Rev. 2001; 101(9):2613-54. DOI: 10.1021/cr990139w. View

Assafim M, Frattani F, Ferreira M, Silva D, Monteiro R, Zingali R . Exploiting the antithrombotic effect of the (pro)thrombin inhibitor bothrojaracin. Toxicon. 2016; 119:46-51. DOI: 10.1016/j.toxicon.2016.05.007. View

10.

Kini R, Doley R . Structure, function and evolution of three-finger toxins: mini proteins with multiple targets. Toxicon. 2010; 56(6):855-67. DOI: 10.1016/j.toxicon.2010.07.010. View

11.

Koivula K, Rondinelli S, Nasman J . The three-finger toxin MTalpha is a selective alpha(2B)-adrenoceptor antagonist. Toxicon. 2010; 56(3):440-7. DOI: 10.1016/j.toxicon.2010.05.001. View

12.

Kini R, Evans H . A model to explain the pharmacological effects of snake venom phospholipases A2. Toxicon. 1989; 27(6):613-35. DOI: 10.1016/0041-0101(89)90013-5. View

13.

Lazarovici P, Marcinkiewicz C, Lelkes P . From Snake Venom's Disintegrins and C-Type Lectins to Anti-Platelet Drugs. Toxins (Basel). 2019; 11(5). PMC: 6563238. DOI: 10.3390/toxins11050303. View

14.

Yang J, Wang D, Jia C, Wang M, Hao G, Yang G . Freely Accessible Chemical Database Resources of Compounds for In Silico Drug Discovery. Curr Med Chem. 2018; 26(42):7581-7597. DOI: 10.2174/0929867325666180508100436. View

15.

Webb B, Sali A . Comparative Protein Structure Modeling Using MODELLER. Curr Protoc Bioinformatics. 2016; 54:5.6.1-5.6.37. PMC: 5031415. DOI: 10.1002/cpbi.3. View

16.

Almeida J, Palacios A, Patino R, Mendes B, Teixeira C, Gomes P . Harnessing snake venom phospholipases A to novel approaches for overcoming antibiotic resistance. Drug Dev Res. 2018; 80(1):68-85. DOI: 10.1002/ddr.21456. View

17.

Volpe M, Rubattu S, Burnett Jr J . Natriuretic peptides in cardiovascular diseases: current use and perspectives. Eur Heart J. 2013; 35(7):419-25. PMC: 4023301. DOI: 10.1093/eurheartj/eht466. View

18.

McDermott A . News Feature: Venom back in vogue as a wellspring for drug candidates. Proc Natl Acad Sci U S A. 2020; 117(19):10100-10104. PMC: 7229657. DOI: 10.1073/pnas.2004486117. View

19.

Scarborough R, Rose J, Hsu M, Phillips D, Fried V, Campbell A . Barbourin. A GPIIb-IIIa-specific integrin antagonist from the venom of Sistrurus m. barbouri. J Biol Chem. 1991; 266(15):9359-62. View

20.

Martins S, Perez M, Moreira I, Sousa S, Ramos M, Fernandes P . Computational Alanine Scanning Mutagenesis: MM-PBSA vs TI. J Chem Theory Comput. 2015; 9(3):1311-9. DOI: 10.1021/ct4000372. View