Studies about Snake Peptides: a Review about Brazilian Contribution

Assis, Rhayane Alves; Bittar, Bruno Barros; Amorim, Nathan Pereira Lima; Carrasco, Guilherme Henrique; Silveira, Elaine Divina Rodrigues; Benvindo‐Souza, Marcelino; Santos, Lia Raquel de Souza

doi:10.1590/1678-4324-2022210421

Cited by 4 publications

(1 citation statement)

References 119 publications

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“…Pyroglutamate peptides have been identified in some animal venoms [ 8 , 13 , 28 , 29 , 30 , 31 , 32 , 33 ]. The prevalence of pyroglutamate-modified peptides is higher in conotoxin [ 8 ] and snake venom [ 34 ], with fewer occurrences in scorpion venoms [ 13 , 33 ]. The generation of pyroglutamic acid at the N-terminus can greatly enhance the blocking effect of toxins for their target channels or stabilize against N-terminal degradation [ 9 ].…”

Section: Resultsmentioning

confidence: 99%

Unveiling the Diversity and Modifications of Short Peptides in Buthus martensii Scorpion Venom through Liquid Chromatography-High Resolution Mass Spectrometry

Zeng,

Zhang,

Yang

et al. 2024

Toxins

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More recently, short peptides in scorpion venom have received much attention because of their potential for drug discovery. Although various biological effects of these short peptides have been found, their studies have been hindered by the lack of structural information especially in modifications. In this study, small peptides from scorpion venom were investigated using high-performance liquid chromatography high-resolution mass spectrometry followed by de novo sequencing. A total of 156 sequences consisting of 2~12 amino acids were temporarily identified from Buthus martensii scorpion venom. The identified peptides exhibited various post-translational modifications including N-terminal and C-terminal modifications, in which the N-benzoyl modification was first found in scorpion venom. Moreover, a short peptide Bz-ARF-NH2 demonstrated both N-terminal and C-terminal modifications simultaneously, which is extremely rare in natural peptides. In conclusion, this study provides a comprehensive insight into the diversity, modifications, and potential bioactivities of short peptides in scorpion venom.

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Section: Resultsmentioning

confidence: 99%

Unveiling the Diversity and Modifications of Short Peptides in Buthus martensii Scorpion Venom through Liquid Chromatography-High Resolution Mass Spectrometry

Zeng,

Zhang,

Yang

et al. 2024

Toxins

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Characterization of a New Hypotensive Peptide from the Venom of Snake Bothrops jararaca (Bj)

Basak,

Carmona,

et al. 2023

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Background: Snake venom has become a key source of many bioactive peptides, enzymes, and toxins associated with blood coagulation and neuronal toxicity. In the past, a number of bradykinin potentiating peptides have been isolated from snake venom that display hypotensive activity due to their inhibitory action towards Angiotensin-Converting Enzyme (ACE). Significant interest has developed to isolate, characterize, and subsequently design peptide analogs as potent ACE-inhibitors which may find therapeutic applications for the treatment of hypertension and associated diseases. Aim: The aim of this study is to search for new bioactive peptide/s in the venom of the snake Bothrops Jararaca (Bj). Objective: The objective is to isolate and characterize new hypotensive peptides from BJ venom. Methods: We examined the venom of Bj which is known to host a range of bioactive peptides. We have isolated a new peptide (BJ-1) which displayed in vitro potent hypotensive activity. The peptide was purified via Sephadex G25 column chromatography and RP-HPLC. It was characterized by mass spectrometry, amino acid analysis, N-terminal sequencing, and chemical synthesis. Result: The peptide was identified as an octa-decapeptide with amino acid sequence as DCPSDWSSYEGHCYKPFS where the two Cys residues are likely present in free state, although they can form an internal S-S bond upon oxidation. It was fully confirmed by comparing with synthetic peptide prepared by solid phase chemistry. Both have the same molecular mass (2,108 Da) and identical bioactivity. Furthermore, we rationalize that BJ-1 may be derived from precursor protein “Coagulation factor IX/factor X binding protein (CF-IX/X-BP)” by proteolytic cleavage at the Nterminus of its B-chain within the sequence KPFS18↓E19PKN. This cleavage site contains the recognition motif of enzyme PCSK8 (Proprotein Convertase Subtilisin Kexin8) also known as Subtilisin Kexin Isozyme 1 (SKI-1) or Site 1 Protease (S1P). Despite this observation, using a synthetic peptide encompassing the proposed cleavage site and recombinant PCSK8 enzyme, we found that the enzyme responsible for generation of BJ-1 is not PCSK8. Further studies will be needed to identify the associated enzyme and fully characterize the pharmacological and biological properties of the peptide. Conclusion: Our study revealed the presence of a novel hypotensive octa-decapeptide in the venom of the snake Bothrops jararaca. It is likely derived from the A-chain of protein CF-IX/X-BP via proteolytic cleavage at the N-terminus by a protease yet to be characterized.

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Past, Present, and Future of Naturally Occurring Antimicrobials Related to Snake Venoms

Oguiura

Sanches

Duarte

et al. 2023

Animals

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This review focuses on proteins and peptides with antimicrobial activity because these biopolymers can be useful in the fight against infectious diseases and to overcome the critical problem of microbial resistance to antibiotics. In fact, snakes show the highest diversification among reptiles, surviving in various environments; their innate immunity is similar to mammals and the response of their plasma to bacteria and fungi has been explored mainly in ecological studies. Snake venoms are a rich source of components that have a variety of biological functions. Among them are proteins like lectins, metalloproteinases, serine proteinases, L-amino acid oxidases, phospholipases type A2, cysteine-rich secretory proteins, as well as many oligopeptides, such as waprins, cardiotoxins, cathelicidins, and β-defensins. In vitro, these biomolecules were shown to be active against bacteria, fungi, parasites, and viruses that are pathogenic to humans. Not only cathelicidins, but all other proteins and oligopeptides from snake venom have been proteolyzed to provide short antimicrobial peptides, or for use as templates for developing a variety of short unnatural sequences based on their structures. In addition to organizing and discussing an expressive amount of information, this review also describes new β-defensin sequences of Sistrurus miliarius that can lead to novel peptide-based antimicrobial agents, using a multidisciplinary approach that includes sequence phylogeny.

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Studies about Snake Peptides: a Review about Brazilian Contribution

Cited by 4 publications

References 119 publications

Unveiling the Diversity and Modifications of Short Peptides in Buthus martensii Scorpion Venom through Liquid Chromatography-High Resolution Mass Spectrometry

Unveiling the Diversity and Modifications of Short Peptides in Buthus martensii Scorpion Venom through Liquid Chromatography-High Resolution Mass Spectrometry

Characterization of a New Hypotensive Peptide from the Venom of Snake Bothrops jararaca (Bj)

Past, Present, and Future of Naturally Occurring Antimicrobials Related to Snake Venoms

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