Closer look into HIV-host interactions: Standard Gibbs energy of binding of the gp120 antigen of HIV-1 to the CD4 receptor and monoclonal antibodies
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HIV-1, like other viruses, represents an open thermodynamic system. This is why it is important to know its thermodynamic properties. Virus-host interactions are performed at the membrane as antigen-receptor binding. Antigen-receptor binding represents a chemical reaction, similar to protein-ligand interactions. The driving force for antigen-receptor binding is Gibbs energy of binding. Knowing Gibbs energy of binding, it is possible to estimate the rate of virus binding and entry into host cells. In this paper, binding equilibrium constants and standard Gibbs energies of binding between the HIV-1 gp120 antigen and the CD4 receptor have been reported at 4 °C, 22 °C and 37 °C.
Keywords:
Biothermodynamics of viruses / HIV-1 / Binding constant / Gibbs energy of binding / Antigen-receptor bindingSource:
Life in Silico, 2023, 1, 1, 8-12Publisher:
- Bektas Tepe Publications
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https://life-insilico.com/index.php/pub/article/view/2https://cer.ihtm.bg.ac.rs/handle/123456789/6136
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IHTMTY - JOUR AU - Popović, Marko PY - 2023 UR - https://life-insilico.com/index.php/pub/article/view/2 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/6136 AB - HIV-1, like other viruses, represents an open thermodynamic system. This is why it is important to know its thermodynamic properties. Virus-host interactions are performed at the membrane as antigen-receptor binding. Antigen-receptor binding represents a chemical reaction, similar to protein-ligand interactions. The driving force for antigen-receptor binding is Gibbs energy of binding. Knowing Gibbs energy of binding, it is possible to estimate the rate of virus binding and entry into host cells. In this paper, binding equilibrium constants and standard Gibbs energies of binding between the HIV-1 gp120 antigen and the CD4 receptor have been reported at 4 °C, 22 °C and 37 °C. PB - Bektas Tepe Publications T2 - Life in Silico T1 - Closer look into HIV-host interactions: Standard Gibbs energy of binding of the gp120 antigen of HIV-1 to the CD4 receptor and monoclonal antibodies VL - 1 IS - 1 SP - 8 EP - 12 UR - https://hdl.handle.net/21.15107/rcub_cer_6136 ER -
@article{ author = "Popović, Marko", year = "2023", abstract = "HIV-1, like other viruses, represents an open thermodynamic system. This is why it is important to know its thermodynamic properties. Virus-host interactions are performed at the membrane as antigen-receptor binding. Antigen-receptor binding represents a chemical reaction, similar to protein-ligand interactions. The driving force for antigen-receptor binding is Gibbs energy of binding. Knowing Gibbs energy of binding, it is possible to estimate the rate of virus binding and entry into host cells. In this paper, binding equilibrium constants and standard Gibbs energies of binding between the HIV-1 gp120 antigen and the CD4 receptor have been reported at 4 °C, 22 °C and 37 °C.", publisher = "Bektas Tepe Publications", journal = "Life in Silico", title = "Closer look into HIV-host interactions: Standard Gibbs energy of binding of the gp120 antigen of HIV-1 to the CD4 receptor and monoclonal antibodies", volume = "1", number = "1", pages = "8-12", url = "https://hdl.handle.net/21.15107/rcub_cer_6136" }
Popović, M.. (2023). Closer look into HIV-host interactions: Standard Gibbs energy of binding of the gp120 antigen of HIV-1 to the CD4 receptor and monoclonal antibodies. in Life in Silico Bektas Tepe Publications., 1(1), 8-12. https://hdl.handle.net/21.15107/rcub_cer_6136
Popović M. Closer look into HIV-host interactions: Standard Gibbs energy of binding of the gp120 antigen of HIV-1 to the CD4 receptor and monoclonal antibodies. in Life in Silico. 2023;1(1):8-12. https://hdl.handle.net/21.15107/rcub_cer_6136 .
Popović, Marko, "Closer look into HIV-host interactions: Standard Gibbs energy of binding of the gp120 antigen of HIV-1 to the CD4 receptor and monoclonal antibodies" in Life in Silico, 1, no. 1 (2023):8-12, https://hdl.handle.net/21.15107/rcub_cer_6136 .