Every year millions of people contract HIV or die from HIV-AIDS related illnesses. Since current drugs generally target viral enzymes, selective drug pressure coupled with the high mutation rate and infidelity of HIV-1 reverse transcriptase lead to drug resistance. It is thus crucial to develop new, tighter-binding inhibitors with more flexible structures that can better inhibit mutant proteases. Two novel inhibitor cores were designed and synthesized, all while attempting to stay within the confines of the substrate-envelope. Many new drugs were tested, which bound to various drug-resistant mutants in the pM range.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Gildemeister, Reinhold Garalt

Colaboradores

• Akbar, Ali

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-042911-162135

Advisor

• Adams, David S.

Year

• 2011

Sponsor

• UMASS Medical Center

Date created

• 2011-04-29

Resource type

• Major Qualifying Project

Major

• Biochemistry
• Biology & Biotechnology

Rights statement

• In Copyright