We DO NOT PROVIDE ANY PRODUCTS OR SERVICES DIRECTLY TO PATIENTS. All of our products are for Research Use Only (RUO), NOT intended for diagnostic, therapeutic, or clinical use.
Anti-monkeypox Drug Discovery Services Targeting Entry/Fusion Protein
Creative Biolab specializes in Monkeypox research. We have over 10 years of experience in providing solutions for rapid anti-Monkeypox drug discovery in the most cost-effective manner.
Entry/Fusion Inhibitors as Antiviral Drug Target
Only five classes of viral targets have been exploited till now for the design of antivirals. Critical steps of the virus life cycle such as cell entry, replication, and assembly of virion need to be explored further for designing antiviral drugs. Attachment of a viral envelope protein to the specific receptor on the host cell membrane, which determines the tropism of the virus, is the first and foremost step in its life cycle. However, it has been largely overlooked as a drug target. However, it has been largely ignored as a drug target. Envelope glycoproteins are the first proteins encountered by the host immune system during infection. They can be potential extracellular drug targets, which makes them relatively accessible. Entry/fusion inhibitors are an important example of a process by which antiviral drugs target non-enzymatic viruses.
Fig.1 Sequence of events in membrane fusion promoted by a viral fusion protein. (Harrison, 2008)
Structural Classification of Viral Fusion Proteins
Viral envelope proteins perform two main functions: binding to specific host receptors and then membrane fusion. In some viruses, single envelope protein performs these two processes as both the receptor binding region and the fusion peptide are present in a single protein forming a homodimer or homotrimer. While most viruses have two different envelope proteins as heterodimers, one for receptor recognition and the other for fusion peptides. Viral fusion proteins can be divided into three types according to their structural characteristics. All viral fusion proteins adopt hairpin structures in their final form. The fusion peptide is bipartite and points to the pre-fusion form of the viral membrane. Viral proteins that mediate membrane fusion vary greatly in structure, fusion triggering mechanism, and fusion peptide types.
Anti-Monkeypox Drug Discovery Services at Creative Biolabs
The broad spectrum of entry/fusion inhibitors includes natural products such as griffithsin protein and squalamine to inhibit viral quantity. Another such compound is the indole-derivative arbidol, which inhibits membrane fusion by conformational changes in the fusion peptide during viral fusion. Structural information and the availability of crystal structure of various viral envelope proteins have proven to be a great advantage in developing inhibitors against them. Class I, II, and III fusion proteins, although structurally different, eventually fold in a similar hairpin structure. Thus, the fusion mechanism of all enveloped viruses may be similar. Therefore, the development of broad-spectrum antivirals targeting the fusion proteins and blocking the entry of various viruses is an important strategy to control many viral infections, including monkeypox.
Creative Biolabs has experienced technical teams and experts that have proven to be a valuable asset to anti-monkeypox drug development projects on many occasions. We will be an extension of your R&D team, ready to meet your drug discovery needs. Please contact us to discuss your anti-monkeypox drug discovery project.