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Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
Published on: August 20, 2018
Design, synthesis and immunological evaluation of novel amphiphilic desmuramyl peptides
Farooq-Ahmad Khan1, Marina Ulanova2, Bing Bai3
1Department of Chemistry, Lakehead University, 955 Oliver Road, Thunder Bay, Ontario, P7B 5E1, Canada; Medical Sciences Division, Northern Ontario School of Medicine, Lakehead University, 955 Oliver Road, Thunder Bay, Ontario, P7B 5E1, Canada.
Abstract:
Muramyl dipeptide (MDP) - an essential bacterial cell wall component - is recognized by our immune system as pathogen-associated molecular pattern (PAMP) which results in immune responses with adverse toxic effects. In order to harness the beneficial properties from the pro-inflammatory characteristics of the bacterial cell wall motif, MDP was strategically re-designed while conserving the L-D configurations of the dipeptide moiety. The muramic acid was replaced with a hydrophilic arene and lipophilic chain was introduced at peptide end to give the amphiphilic desmuramyl peptides (DMPs). The novel DMPs were found to modulate the immune response by amplifying the LPS-induced surface glycoprotein (ICAM-1) expression in THP-1 cells without showing significant toxicity. Furthermore, these compounds were able to trigger the secretion of higher levels of pro-inflammatory cytokine (TNF-α) than the well-studied NOD2 agonist, Murabutide.
Insights
Novel desmuramyl peptides (DMPs) were designed to harness beneficial immune responses from bacterial components. These DMPs amplify immune signaling without toxicity, offering a promising therapeutic avenue.
Area of Science:
- Immunology
- Medicinal Chemistry
Background:
- Muramyl dipeptide (MDP) is a bacterial cell wall component recognized as a pathogen-associated molecular pattern (PAMP).
- MDP triggers immune responses but can cause adverse toxic effects.
- Re-designing MDP aims to harness its beneficial pro-inflammatory properties while mitigating toxicity.
Purpose of the Study:
- To develop novel desmuramyl peptides (DMPs) by modifying the MDP structure.
- To evaluate the immunomodulatory effects and toxicity of these DMPs.
- To compare DMP efficacy with existing immune agonists like Murabutide.
Main Methods:
- Strategic re-design of MDP, replacing muramic acid with a hydrophilic arene and adding a lipophilic chain.
- Assessing DMP effects on lipopolysaccharide (LPS)-induced intercellular adhesion molecule 1 (ICAM-1) expression in THP-1 cells.
- Measuring pro-inflammatory cytokine (TNF-α) secretion in response to DMPs.
Main Results:
- Novel DMPs successfully modulated immune responses.
- DMPs amplified LPS-induced ICAM-1 expression in THP-1 cells without significant toxicity.
- DMPs induced higher levels of TNF-α secretion compared to Murabutide.
Conclusions:
- Amphiphilic DMPs represent a promising class of immunomodulatory compounds.
- DMPs offer a strategy to leverage bacterial component-derived immune stimulation safely.
- These findings suggest potential therapeutic applications for DMPs in modulating immune responses.
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