Analyzing HIV-1 Dynamics through Michaelis-Menten Framework

The Michaelis-Menten equation describes the kinetics of enzymatic reactions,

demystifying the relationship between reaction rates and the concentrations of

enzymes and substrates. This is essential in biochemistry for understanding and

quantifying enzyme-substrate interactions.

Originating from the work of biochemists Leonor Michaelis and Maud Menten, the

significance reverberates from laundry detergents, environmental cleanup,

biotechnology, medical treatments, and food production to contemporary research,

particularly in studies centred on human immunodeficiency virus (HIV-1).

In some recent HIV investigations, researchers utilised Michaelis-Menten kinetics to

enhance comprehension and assay sensitivity. One study devised an advanced

assay employing a novel substrate, Substrate 1, purified through high-performance

liquid chromatography. When applied to assess HIV-1 protease inhibitors, this

approach improved sensitivity and kinetic parameters, offering insights into the

dynamics of HIV protease activity.

Another study delved into functional curability in HIV infection and used a

mathematical framework akin to the Michaelis-Menten equation. This investigation

explored the nuanced interplay between immune response dynamics and viral load

reduction, defining conditions for a potential functional cure.

Whether applied to protease inhibition or unravelling the intricacies of viral dynamics,

the Michaelis-Menten equation continues to guide researchers towards more

nuanced approaches in the ongoing quest to combat HIV.

Chen, J.-H. (2017) An analysis of functional curability on HIV infection models with

michaelis-menten-type immune response and its generalization, Discrete and

Continuous Dynamical Systems - B. Available at:

2024).

Windsor, I.W. and Raines, R.T. (2015) Fluorogenic assay for inhibitors of HIV-1 protease

with sub-picomolar affinity, Nature News. Available at:

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