Special Issue "Proteomics Analysis in Animal Venom"

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

Deadline for manuscript submissions: closed (31 March 2021) | Viewed by 3015

Special Issue Editor

Prof. Dr. Paul Long
E-Mail Website
Guest Editor
Faculty of Life Sciences & Medicine, King’s College London, United Kingdom & Faculdade de Ciências Farmacêuticas, Universidade de São Paulo, Brazil
Interests: proteomics; animal venom
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

A basic issue for animals is how to win-out survival competitions by balancing trade-offs and trait modifications necessary for predation and those intended for defence. Venomous animals can use toxins to mediate both key processes, thus shifts between being the hunter towards being the hunted and vice versa, might be expected to alter venom composition. Our understanding of the dual-purpose nature of toxin chemistry has significantly expanded over recent years because of improvements in modern instrumentation that supports large-scale measurement of venom proteomes. In this Special Issue, manuscripts that describe proteomics approaches offering critical insights into the following themes are especially welcome:

  • Comparative study of toxins in poorly studied venomous animals.
  • Adaptiveplasticity in venom composition related to animal behaviour or ecology.
  • Integrating de novo peptide sequencing with annotation methods to assign the sequence to tandem mass spectra that are routinely discarded.
  • Informatics methods to extract biological value from sequences by linkage to multiple biological, chemical and literature resources.
  • Pharmaceutical discovery of novel therapeutic peptides.

Prof. Dr. Paul Long
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2400 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Gel electrophoresis
  • mass spectrometry (MS, MS/MS, LC-MS
  • proteome database
  • protein quantitation
  • orthology prediction
  • functional annotation
  • sequence analysis

Published Papers (1 paper)

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Research

Article
Aspartic Acid Isomerization Characterized by High Definition Mass Spectrometry Significantly Alters the Bioactivity of a Novel Toxin from Poecilotheria
Toxins 2020, 12(4), 207; https://doi.org/10.3390/toxins12040207 - 25 Mar 2020
Cited by 1 | Viewed by 2453
Abstract
Research in toxinology has created a pharmacological paradox. With an estimated 220,000 venomous animals worldwide, the study of peptidyl toxins provides a vast number of effector molecules. However, due to the complexity of the protein-protein interactions, there are fewer than ten venom-derived molecules [...] Read more.
Research in toxinology has created a pharmacological paradox. With an estimated 220,000 venomous animals worldwide, the study of peptidyl toxins provides a vast number of effector molecules. However, due to the complexity of the protein-protein interactions, there are fewer than ten venom-derived molecules on the market. Structural characterization and identification of post-translational modifications are essential to develop biological lead structures into pharmaceuticals. Utilizing advancements in mass spectrometry, we have created a high definition approach that fuses conventional high-resolution MS-MS with ion mobility spectrometry (HDMSE) to elucidate these primary structure characteristics. We investigated venom from ten species of “tiger” spider (Genus: Poecilotheria) and discovered they contain isobaric conformers originating from non-enzymatic Asp isomerization. One conformer pair conserved in five of ten species examined, denominated PcaTX-1a and PcaTX-1b, was found to be a 36-residue peptide with a cysteine knot, an amidated C-terminus, and isoAsp33Asp substitution. Although the isomerization of Asp has been implicated in many pathologies, this is the first characterization of Asp isomerization in a toxin and demonstrates the isomerized product’s diminished physiological effects. This study establishes the value of a HDMSE approach to toxin screening and characterization. Full article
(This article belongs to the Special Issue Proteomics Analysis in Animal Venom)
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