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We take viruses apart.
We put them back together.
We make them make mistakes.

The Zlotnick lab dissects virus assembly using a broad array of biophysical and biochemical tools. We perturb “normal” assembly with mutants and small molecules. Results of perturbations are observed in vitro and in cells. Changes in structure are correlated with changes in assembly.

Assembly-directed small molecules can be antivirals. Our small molecules speed up assembly by orders of magnitude. How can this be antiviral? Imagine an assembly line, producing cars or viruses. It moves at a relatively slow rate and different pieces are added one at a time. If we accelerate the assembly line a little bit, say twofold, we get more cars but also more mistakes. If we accelerate the assembly line 100-fold, say from ¼ mile and hour to 25 miles an hour, we’ll be lucky to get a steering wheel.

Recent News

Nora Gibes receives Peglow Award for International HBV Meeting

Congratulations to Nora Gibes! She is the recipient of a Peglow Award for travel to the 2022 International HBV Meeting in Paris, France from September 18-22, 2022.

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Congratulations to Patrick Laughlin on being awarded Graduate Fellowship

We are delighted to announce that graduate student, Patrick Laughlin, has been awarded a Quantitative Chemical Biology Graduate Fellowship.

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Assembly Biosciences and Door Pharmaceuticals sign agreement to collaborate on development of a novel class of HBV core protein modulators.

SOUTH SAN FRANCISCO, Calif., Nov. 16, 2020 (GLOBE NEWSWIRE) -- Assembly Biosciences, Inc. (Nasdaq: ASMB) and Door Pharmaceuticals, LLC today announced that the companies have signed an exclusive, two-year collaboration and option agreement focused on the development of a novel class of hepatitis B virus (HBV) core protein modulators. Door Pharmaceuticals’ innovative discovery platform targets…

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These overlays show comparisons of Hepatitis B Virus capsids with bound drugs (purple) to a normal capsid without drug (green). Though the drugs, HAP1, HAP18, and AT130, each bind to different sites, their effects on capsid structure are distinctly different. (This figure was made by Bala Venkatakrishnan.)

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