Identification of natural antimicrobial peptides mimetic to inhibit Ca2+ influx DDX3X activity for blocking dengue viral infectivity.
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| Title: | Identification of natural antimicrobial peptides mimetic to inhibit Ca2+ influx DDX3X activity for blocking dengue viral infectivity. |
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| Authors: | Asseri, Amer H.1,2 (AUTHOR) ahasseri@kau.edu.sa, Islam, Md Rashedul1,3 (AUTHOR), Alghamdi, Reem M.4 (AUTHOR), Altayb, Hisham N.1,2 (AUTHOR) |
| Source: | Journal of Bioenergetics & Biomembranes. Apr2024, Vol. 56 Issue 2, p125-139. 15p. |
| Subjects: | Antimicrobial peptides, Dengue viruses, RNA metabolism, Peptides, Dengue, Drug discovery, Camel milk |
| Abstract: | Viruses are microscopic biological entities that can quickly invade and multiply in a living organism. Each year, over 36,000 people die and nearly 400 million are infected with the dengue virus (DENV). Despite dengue being an endemic disease, no targeted and effective antiviral peptide resource is available against the dengue species. Antiviral peptides (AVPs) have shown tremendous ability to fight against different viruses. Accelerating antiviral drug discovery is crucial, particularly for RNA viruses. DDX3X, a vital cell component, supports viral translation and interacts with TRPV4, regulating viral RNA metabolism and infectivity. Its diverse signaling pathway makes it a potential therapeutic target. Our study focuses on inhibiting viral RNA translation by blocking the activity of the target gene and the TRPV4-mediated Ca2+ cation channel. Six major proteins from camel milk were first extracted and split with the enzyme pepsin. The antiviral properties were then analyzed using online bioinformatics programs, including AVPpred, Meta-iAVP, AMPfun, and ENNAVIA. The stability of the complex was assessed using MD simulation, MM/GBSA, and principal component analysis. Cytotoxicity evaluations were conducted using COPid and ToxinPred. The top ten AVPs, determined by optimal scores, were selected and saved for docking studies with the GalaxyPepDock tools. Bioinformatics analyses revealed that the peptides had very short hydrogen bond distances (1.8 to 3.6 Å) near the active site of the target protein. Approximately 76% of the peptide residues were 5–11 amino acids long. Additionally, the identified peptide candidates exhibited desirable properties for potential therapeutic agents, including a net positive charge, moderate toxicity, hydrophilicity, and selectivity. In conclusion, this computational study provides promising insights for discovering peptide-based therapeutic agents against DENV. [ABSTRACT FROM AUTHOR] |
| Copyright of Journal of Bioenergetics & Biomembranes is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
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| Header | DbId: egs DbLabel: Engineering Source An: 176453044 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Identification of natural antimicrobial peptides mimetic to inhibit Ca<superscript>2+</superscript> influx DDX3X activity for blocking dengue viral infectivity. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Asseri%2C+Amer+H%2E%22">Asseri, Amer H.</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<i> ahasseri@kau.edu.sa</i><br /><searchLink fieldCode="AR" term="%22Islam%2C+Md+Rashedul%22">Islam, Md Rashedul</searchLink><relatesTo>1,3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Alghamdi%2C+Reem+M%2E%22">Alghamdi, Reem M.</searchLink><relatesTo>4</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Altayb%2C+Hisham+N%2E%22">Altayb, Hisham N.</searchLink><relatesTo>1,2</relatesTo> (AUTHOR) – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Journal+of+Bioenergetics+%26+Biomembranes%22">Journal of Bioenergetics & Biomembranes</searchLink>. Apr2024, Vol. 56 Issue 2, p125-139. 15p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Antimicrobial+peptides%22">Antimicrobial peptides</searchLink><br /><searchLink fieldCode="DE" term="%22Dengue+viruses%22">Dengue viruses</searchLink><br /><searchLink fieldCode="DE" term="%22RNA+metabolism%22">RNA metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Peptides%22">Peptides</searchLink><br /><searchLink fieldCode="DE" term="%22Dengue%22">Dengue</searchLink><br /><searchLink fieldCode="DE" term="%22Drug+discovery%22">Drug discovery</searchLink><br /><searchLink fieldCode="DE" term="%22Camel+milk%22">Camel milk</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Viruses are microscopic biological entities that can quickly invade and multiply in a living organism. Each year, over 36,000 people die and nearly 400 million are infected with the dengue virus (DENV). Despite dengue being an endemic disease, no targeted and effective antiviral peptide resource is available against the dengue species. Antiviral peptides (AVPs) have shown tremendous ability to fight against different viruses. Accelerating antiviral drug discovery is crucial, particularly for RNA viruses. DDX3X, a vital cell component, supports viral translation and interacts with TRPV4, regulating viral RNA metabolism and infectivity. Its diverse signaling pathway makes it a potential therapeutic target. Our study focuses on inhibiting viral RNA translation by blocking the activity of the target gene and the TRPV4-mediated Ca2+ cation channel. Six major proteins from camel milk were first extracted and split with the enzyme pepsin. The antiviral properties were then analyzed using online bioinformatics programs, including AVPpred, Meta-iAVP, AMPfun, and ENNAVIA. The stability of the complex was assessed using MD simulation, MM/GBSA, and principal component analysis. Cytotoxicity evaluations were conducted using COPid and ToxinPred. The top ten AVPs, determined by optimal scores, were selected and saved for docking studies with the GalaxyPepDock tools. Bioinformatics analyses revealed that the peptides had very short hydrogen bond distances (1.8 to 3.6 Å) near the active site of the target protein. Approximately 76% of the peptide residues were 5–11 amino acids long. Additionally, the identified peptide candidates exhibited desirable properties for potential therapeutic agents, including a net positive charge, moderate toxicity, hydrophilicity, and selectivity. In conclusion, this computational study provides promising insights for discovering peptide-based therapeutic agents against DENV. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Journal of Bioenergetics & Biomembranes is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1007/s10863-023-09996-1 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 15 StartPage: 125 Subjects: – SubjectFull: Antimicrobial peptides Type: general – SubjectFull: Dengue viruses Type: general – SubjectFull: RNA metabolism Type: general – SubjectFull: Peptides Type: general – SubjectFull: Dengue Type: general – SubjectFull: Drug discovery Type: general – SubjectFull: Camel milk Type: general Titles: – TitleFull: Identification of natural antimicrobial peptides mimetic to inhibit Ca2+ influx DDX3X activity for blocking dengue viral infectivity. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Asseri, Amer H. – PersonEntity: Name: NameFull: Islam, Md Rashedul – PersonEntity: Name: NameFull: Alghamdi, Reem M. – PersonEntity: Name: NameFull: Altayb, Hisham N. IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 04 Text: Apr2024 Type: published Y: 2024 Identifiers: – Type: issn-print Value: 0145479X Numbering: – Type: volume Value: 56 – Type: issue Value: 2 Titles: – TitleFull: Journal of Bioenergetics & Biomembranes Type: main |
| ResultId | 1 |
