Volker Herzig , Andrew Ahabh , Alun Jones , Glenn F. King
{"title":"Shining a light on the photochemical stability of peptidic bioinsecticides","authors":"Volker Herzig , Andrew Ahabh , Alun Jones , Glenn F. King","doi":"10.1016/j.toxicon.2025.108381","DOIUrl":null,"url":null,"abstract":"<div><div>Peptide toxins from spider venoms are being increasingly hailed as environmentally friendly alternatives to market-dominating small-molecule chemical insecticides. While the stability of knotted spider-venom peptides towards enzymatic degradation, temperature changes and varying pH conditions has already been examined, their susceptibility to sunlight remains unclear. Field applications of insecticides demand that the insecticidal component is active for at least a few days to ensure sufficient eradication of the targeted insect pests. We therefore exposed four insecticidal spider-venom peptides (ω-Hv1a, ω/κ-Hv1a, Ta1a and Dc1a) to continuous artificial sunlight for up to 7 days. After certain incubation periods, we quantified the percentage of intact peptide and identified sites of peptide cleavage. We found that after 3 days of continuous exposure (=6 days of 12 h/d sunlight), the amount of remaining intact peptide was 16 % (Ta1a), 21 % (Dc1a), 55 % (ω-Hv1a), and 67 % (ω/κ-Hv1a), whereas bovine serum albumin was completely degraded. Even after 7 days (=14 days of 12 h/d sunlight) exposure, more than 50 % of ω/κ-Hv1a and ω-Hv1a remained intact. Peptides with lower molecular mass tended to be less susceptible to sunlight, while cleavage of peptide bonds involving proline or cysteine were most susceptible to photochemical degradation. The photochemical changes detected by mass spectrometry mainly comprised oxidations, deamidations, and cysteine-targeted modifications.</div></div>","PeriodicalId":23289,"journal":{"name":"Toxicon","volume":"262 ","pages":"Article 108381"},"PeriodicalIF":2.6000,"publicationDate":"2025-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Toxicon","FirstCategoryId":"3","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0041010125001552","RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"PHARMACOLOGY & PHARMACY","Score":null,"Total":0}
引用次数: 0
Abstract
Peptide toxins from spider venoms are being increasingly hailed as environmentally friendly alternatives to market-dominating small-molecule chemical insecticides. While the stability of knotted spider-venom peptides towards enzymatic degradation, temperature changes and varying pH conditions has already been examined, their susceptibility to sunlight remains unclear. Field applications of insecticides demand that the insecticidal component is active for at least a few days to ensure sufficient eradication of the targeted insect pests. We therefore exposed four insecticidal spider-venom peptides (ω-Hv1a, ω/κ-Hv1a, Ta1a and Dc1a) to continuous artificial sunlight for up to 7 days. After certain incubation periods, we quantified the percentage of intact peptide and identified sites of peptide cleavage. We found that after 3 days of continuous exposure (=6 days of 12 h/d sunlight), the amount of remaining intact peptide was 16 % (Ta1a), 21 % (Dc1a), 55 % (ω-Hv1a), and 67 % (ω/κ-Hv1a), whereas bovine serum albumin was completely degraded. Even after 7 days (=14 days of 12 h/d sunlight) exposure, more than 50 % of ω/κ-Hv1a and ω-Hv1a remained intact. Peptides with lower molecular mass tended to be less susceptible to sunlight, while cleavage of peptide bonds involving proline or cysteine were most susceptible to photochemical degradation. The photochemical changes detected by mass spectrometry mainly comprised oxidations, deamidations, and cysteine-targeted modifications.
期刊介绍:
Toxicon has an open access mirror Toxicon: X, sharing the same aims and scope, editorial team, submission system and rigorous peer review. An introductory offer Toxicon: X - full waiver of the Open Access fee.
Toxicon''s "aims and scope" are to publish:
-articles containing the results of original research on problems related to toxins derived from animals, plants and microorganisms
-papers on novel findings related to the chemical, pharmacological, toxicological, and immunological properties of natural toxins
-molecular biological studies of toxins and other genes from poisonous and venomous organisms that advance understanding of the role or function of toxins
-clinical observations on poisoning and envenoming where a new therapeutic principle has been proposed or a decidedly superior clinical result has been obtained.
-material on the use of toxins as tools in studying biological processes and material on subjects related to venom and antivenom problems.
-articles on the translational application of toxins, for example as drugs and insecticides
-epidemiological studies on envenoming or poisoning, so long as they highlight a previously unrecognised medical problem or provide insight into the prevention or medical treatment of envenoming or poisoning. Retrospective surveys of hospital records, especially those lacking species identification, will not be considered for publication. Properly designed prospective community-based surveys are strongly encouraged.
-articles describing well-known activities of venoms, such as antibacterial, anticancer, and analgesic activities of arachnid venoms, without any attempt to define the mechanism of action or purify the active component, will not be considered for publication in Toxicon.
-review articles on problems related to toxinology.
To encourage the exchange of ideas, sections of the journal may be devoted to Short Communications, Letters to the Editor and activities of the affiliated societies.