What question did this study set out to answer?

Determine whether HIV-1 protease can template the assembly of its own potent inhibitor from weakly binding azide and alkyne precursors using in situ click chemistry.

January 20, 2006Angewandte Chemie International Edition

Inhibitors of HIV‐1 Protease by Using In Situ Click Chemistry

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Authors

MWMatthew Whiting JMJohn Muldoon YLYing‐Chuan Lin

Discussion

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Overview

Biochemical study demonstrates the assembly of potent inhibitors in HIV-1 protease, suggesting that target-templated click chemistry can produce high-affinity therapeutics.

Key Points

Determine whether HIV-1 protease can template the assembly of its own potent inhibitor from weakly binding azide and alkyne precursors using in situ click chemistry.
Incubated HIV-1 protease with complementary azide- and alkyne-containing chemical building blocks.
Facilitated target-guided synthesis to allow the enzyme active site to direct the formation of a triazole linkage between the fragments.
HIV-1 protease successfully catalyzed the coupling of the azide- and alkyne-bearing building blocks via triazole formation.
The newly assembled triazole conjugate exhibited potent inhibitory activity against HIV-1 protease despite the precursor fragments showing poor individual binding affinities.

Cite This Study

Whiting et al. (2006) studied this question.

synapsesocial.com/papers/6a7285a835aa2c282ce34bdd https://doi.org/10.1002/anie.200502161

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January 20, 2006Angewandte Chemie International Edition

Inhibitors of HIV‐1 Protease by Using In Situ Click Chemistry

View Full Paper

Ask AI

Bookmark

Authors

MWMatthew Whiting JMJohn Muldoon YLYing‐Chuan Lin

Discussion

Member takes

Overview

Biochemical study demonstrates the assembly of potent inhibitors in HIV-1 protease, suggesting that target-templated click chemistry can produce high-affinity therapeutics.

Key Points

Determine whether HIV-1 protease can template the assembly of its own potent inhibitor from weakly binding azide and alkyne precursors using in situ click chemistry.
Incubated HIV-1 protease with complementary azide- and alkyne-containing chemical building blocks.
Facilitated target-guided synthesis to allow the enzyme active site to direct the formation of a triazole linkage between the fragments.
HIV-1 protease successfully catalyzed the coupling of the azide- and alkyne-bearing building blocks via triazole formation.
The newly assembled triazole conjugate exhibited potent inhibitory activity against HIV-1 protease despite the precursor fragments showing poor individual binding affinities.

Cite This Study

Whiting et al. (2006) studied this question.

synapsesocial.com/papers/6a7285a835aa2c282ce34bdd https://doi.org/10.1002/anie.200502161

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