Fusion peptide induced modification of membrane organization and dynamics: Implications in developing fusion inhibitors
An essential step in the entrance of enveloped viruses such as coronaviruses, the human immunodeficiency virus, and influenza is membrane fusion. A unique class of glycoprotein found on the viral envelope, known as a fusion protein, is responsible for catalyzing the fusion between the viral envelope...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2023-12-01
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| Series: | Chemical Physics Impact |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2667022423001275 |
| _version_ | 1797400835037069312 |
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| author | Smruti Mishra Manbit Subhadarsi Panda Hirak Chakraborty |
| author_facet | Smruti Mishra Manbit Subhadarsi Panda Hirak Chakraborty |
| author_sort | Smruti Mishra |
| collection | DOAJ |
| description | An essential step in the entrance of enveloped viruses such as coronaviruses, the human immunodeficiency virus, and influenza is membrane fusion. A unique class of glycoprotein found on the viral envelope, known as a fusion protein, is responsible for catalyzing the fusion between the viral envelope and the host cell. Efforts have been made to block the fusion vis-à-vis the entry process by inactivating the fusion protein utilizing peptides and small molecules. Interestingly, the fusion proteins do not have any structural and sequence homology across viruses, and this limited the use of inhibitory peptides against a specific virus causing a paucity of immediate solutions against emerging and re-emerging viral diseases. Therefore, research has been initiated to develop broad-spectrum fusion inhibitors that can be effective to inhibit the entry of many viruses. In this review, we have examined the mechanistic details of membrane fusion and the potential significance of lipid composition. Moreover, we discussed the rationale for developing peptide-based, broad-spectrum fusion inhibitors that target membrane physical characteristics instead of fusion protein inactivation. |
| first_indexed | 2024-03-09T02:01:22Z |
| format | Article |
| id | doaj.art-011ac20cbcd0443585eefafa9faf3b5f |
| institution | Directory Open Access Journal |
| issn | 2667-0224 |
| language | English |
| last_indexed | 2024-03-09T02:01:22Z |
| publishDate | 2023-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Chemical Physics Impact |
| spelling | doaj.art-011ac20cbcd0443585eefafa9faf3b5f2023-12-08T04:46:30ZengElsevierChemical Physics Impact2667-02242023-12-017100287Fusion peptide induced modification of membrane organization and dynamics: Implications in developing fusion inhibitorsSmruti Mishra0Manbit Subhadarsi Panda1Hirak Chakraborty2School of Chemistry, Sambalpur University, Jyoti Vihar, Burla, Odisha 768 019, IndiaSchool of Chemistry, Sambalpur University, Jyoti Vihar, Burla, Odisha 768 019, IndiaCorresponding author.; School of Chemistry, Sambalpur University, Jyoti Vihar, Burla, Odisha 768 019, IndiaAn essential step in the entrance of enveloped viruses such as coronaviruses, the human immunodeficiency virus, and influenza is membrane fusion. A unique class of glycoprotein found on the viral envelope, known as a fusion protein, is responsible for catalyzing the fusion between the viral envelope and the host cell. Efforts have been made to block the fusion vis-à-vis the entry process by inactivating the fusion protein utilizing peptides and small molecules. Interestingly, the fusion proteins do not have any structural and sequence homology across viruses, and this limited the use of inhibitory peptides against a specific virus causing a paucity of immediate solutions against emerging and re-emerging viral diseases. Therefore, research has been initiated to develop broad-spectrum fusion inhibitors that can be effective to inhibit the entry of many viruses. In this review, we have examined the mechanistic details of membrane fusion and the potential significance of lipid composition. Moreover, we discussed the rationale for developing peptide-based, broad-spectrum fusion inhibitors that target membrane physical characteristics instead of fusion protein inactivation.http://www.sciencedirect.com/science/article/pii/S2667022423001275Membrane fusionViral entryFusion inhibitorsMembrane orderMembrane polarity |
| spellingShingle | Smruti Mishra Manbit Subhadarsi Panda Hirak Chakraborty Fusion peptide induced modification of membrane organization and dynamics: Implications in developing fusion inhibitors Chemical Physics Impact Membrane fusion Viral entry Fusion inhibitors Membrane order Membrane polarity |
| title | Fusion peptide induced modification of membrane organization and dynamics: Implications in developing fusion inhibitors |
| title_full | Fusion peptide induced modification of membrane organization and dynamics: Implications in developing fusion inhibitors |
| title_fullStr | Fusion peptide induced modification of membrane organization and dynamics: Implications in developing fusion inhibitors |
| title_full_unstemmed | Fusion peptide induced modification of membrane organization and dynamics: Implications in developing fusion inhibitors |
| title_short | Fusion peptide induced modification of membrane organization and dynamics: Implications in developing fusion inhibitors |
| title_sort | fusion peptide induced modification of membrane organization and dynamics implications in developing fusion inhibitors |
| topic | Membrane fusion Viral entry Fusion inhibitors Membrane order Membrane polarity |
| url | http://www.sciencedirect.com/science/article/pii/S2667022423001275 |
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