Design and Binding Affinity of Antisense Peptides for Snake Venom Neutralization

Snakebites are a significant public health problem in many tropical and subtropical regions, causing extensive morbidity and mortality. Traditional snake antivenoms face multiple challenges, including allergenicity, high production costs, and logistical difficulties, highlighting the urgent need for...

Full description

Saved in:
Bibliographic Details
Main Authors: Ivan Biruš, Tino Šeba, Marin Marić, Mario Gabričević, Tin Weitner
Format: Article
Language:English
Published: MDPI AG 2025-02-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/30/4/903
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1850080707349577728
author Ivan Biruš
Tino Šeba
Marin Marić
Mario Gabričević
Tin Weitner
author_facet Ivan Biruš
Tino Šeba
Marin Marić
Mario Gabričević
Tin Weitner
author_sort Ivan Biruš
collection DOAJ
description Snakebites are a significant public health problem in many tropical and subtropical regions, causing extensive morbidity and mortality. Traditional snake antivenoms face multiple challenges, including allergenicity, high production costs, and logistical difficulties, highlighting the urgent need for new therapeutic approaches. This pilot study explores the potential of oligopeptides as therapeutic inhibitors targeting the neurotoxic sites of ammodytoxin A (AtxA; PDB: 3G8G) from <i>Vipera ammodytes</i>. We selected two sense oligopeptides to represent critical neurotoxic regions of AtxA as targets for inhibition by complementary antisense peptides. Utilizing a heuristic antisense peptide design based on the molecular recognition theory, we modeled two antisense oligopeptides as complementary counterparts for each sense oligopeptide. The modeled sense and antisense peptides were commercially synthesized, and their binding affinities were evaluated using spectrofluorometric titrations. The determined dissociation constants (<i>K</i><sub>D</sub>) were in the range of 1–10 μM for all sense–antisense pairs, revealing relatively strong binding affinities. Confirmation of sense–antisense peptide binding prompted further investigation into their potential binding to the native target protein through global docking simulations using the HPEPDOCK web server. The results highlight the applicability of molecular recognition theory in the development of antisense peptides that could change therapeutic strategies in various biomedical fields. Further studies are needed to investigate the therapeutic efficacy and broader applications of these peptides.
format Article
id doaj-art-748cebbfe6624fb5a697643901bf2bdf
institution DOAJ
issn 1420-3049
language English
publishDate 2025-02-01
publisher MDPI AG
record_format Article
series Molecules
spelling doaj-art-748cebbfe6624fb5a697643901bf2bdf2025-08-20T02:44:53ZengMDPI AGMolecules1420-30492025-02-0130490310.3390/molecules30040903Design and Binding Affinity of Antisense Peptides for Snake Venom NeutralizationIvan Biruš0Tino Šeba1Marin Marić2Mario Gabričević3Tin Weitner4Department of General and Inorganic Chemistry, University of Zagreb Faculty of Pharmacy and Biochemistry, A. Kovačića 1, 10000 Zagreb, CroatiaDepartment of General and Inorganic Chemistry, University of Zagreb Faculty of Pharmacy and Biochemistry, A. Kovačića 1, 10000 Zagreb, CroatiaDepartment of General and Inorganic Chemistry, University of Zagreb Faculty of Pharmacy and Biochemistry, A. Kovačića 1, 10000 Zagreb, CroatiaDepartment of General and Inorganic Chemistry, University of Zagreb Faculty of Pharmacy and Biochemistry, A. Kovačića 1, 10000 Zagreb, CroatiaDepartment of General and Inorganic Chemistry, University of Zagreb Faculty of Pharmacy and Biochemistry, A. Kovačića 1, 10000 Zagreb, CroatiaSnakebites are a significant public health problem in many tropical and subtropical regions, causing extensive morbidity and mortality. Traditional snake antivenoms face multiple challenges, including allergenicity, high production costs, and logistical difficulties, highlighting the urgent need for new therapeutic approaches. This pilot study explores the potential of oligopeptides as therapeutic inhibitors targeting the neurotoxic sites of ammodytoxin A (AtxA; PDB: 3G8G) from <i>Vipera ammodytes</i>. We selected two sense oligopeptides to represent critical neurotoxic regions of AtxA as targets for inhibition by complementary antisense peptides. Utilizing a heuristic antisense peptide design based on the molecular recognition theory, we modeled two antisense oligopeptides as complementary counterparts for each sense oligopeptide. The modeled sense and antisense peptides were commercially synthesized, and their binding affinities were evaluated using spectrofluorometric titrations. The determined dissociation constants (<i>K</i><sub>D</sub>) were in the range of 1–10 μM for all sense–antisense pairs, revealing relatively strong binding affinities. Confirmation of sense–antisense peptide binding prompted further investigation into their potential binding to the native target protein through global docking simulations using the HPEPDOCK web server. The results highlight the applicability of molecular recognition theory in the development of antisense peptides that could change therapeutic strategies in various biomedical fields. Further studies are needed to investigate the therapeutic efficacy and broader applications of these peptides.https://www.mdpi.com/1420-3049/30/4/903snake venompeptide designbinding affinityfluorescence spectroscopymolecular docking
spellingShingle Ivan Biruš
Tino Šeba
Marin Marić
Mario Gabričević
Tin Weitner
Design and Binding Affinity of Antisense Peptides for Snake Venom Neutralization
Molecules
snake venom
peptide design
binding affinity
fluorescence spectroscopy
molecular docking
title Design and Binding Affinity of Antisense Peptides for Snake Venom Neutralization
title_full Design and Binding Affinity of Antisense Peptides for Snake Venom Neutralization
title_fullStr Design and Binding Affinity of Antisense Peptides for Snake Venom Neutralization
title_full_unstemmed Design and Binding Affinity of Antisense Peptides for Snake Venom Neutralization
title_short Design and Binding Affinity of Antisense Peptides for Snake Venom Neutralization
title_sort design and binding affinity of antisense peptides for snake venom neutralization
topic snake venom
peptide design
binding affinity
fluorescence spectroscopy
molecular docking
url https://www.mdpi.com/1420-3049/30/4/903
work_keys_str_mv AT ivanbirus designandbindingaffinityofantisensepeptidesforsnakevenomneutralization
AT tinoseba designandbindingaffinityofantisensepeptidesforsnakevenomneutralization
AT marinmaric designandbindingaffinityofantisensepeptidesforsnakevenomneutralization
AT mariogabricevic designandbindingaffinityofantisensepeptidesforsnakevenomneutralization
AT tinweitner designandbindingaffinityofantisensepeptidesforsnakevenomneutralization