Understanding Drug Resistance in HIV-1 Protease
Author Information
Author(s): Ali Akbar, Bandaranayake Rajintha M., Cai Yufeng, King Nancy M., Kolli Madhavi, Mittal Seema, Murzycki Jennifer F., Nalam Madhavi N.L., Nalivaika Ellen A., Özen Ayşegül, Prabu-Jeyabalan Moses M., Thayer Kelly, Schiffer Celia A.
Primary Institution: University of Massachusetts Medical School
Hypothesis
How do mutations in HIV-1 protease contribute to drug resistance?
Conclusion
The study reveals that mutations in HIV-1 protease can alter inhibitor binding while maintaining the virus's ability to process its natural substrates.
Supporting Evidence
- HIV-1 protease is a major target for antiviral drugs.
- Nine FDA-approved protease inhibitors have been developed using structure-based drug design.
- Mutations in HIV-1 protease can lead to drug resistance while maintaining viral fitness.
- New strategies are needed to design inhibitors that are less susceptible to resistance.
Takeaway
HIV-1 can change its shape to avoid being stopped by medicines, making it harder to treat. Scientists are trying to design better drugs that can still work even when the virus changes.
Methodology
The study reviews structural data and drug design strategies related to HIV-1 protease inhibitors.
Limitations
The study primarily focuses on structural insights and may not cover all clinical implications of drug resistance.
Digital Object Identifier (DOI)
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