David Sherman

Our Research

Composed of a dynamic, interdisciplinary team of scientists, the Sherman laboratory studies the biosynthesis of natural products from microbes that include cyanobacteria, actinomycetes, and myxobacteria. We are inspired by natural products from both terrestrial and marine organisms and seek to better understand their origins using a set of tools that includes molecular biology, genetics, biochemistry, structural biology, and bioorganic chemistry.

About David Sherman

  • Synthetic chemistry
  • Marine microorganisms
  • Drug discovery

David Sherman explores the biochemical pathways of marine microorganisms with the goal of finding new drug candidates for infectious diseases and cancers. He collects samples from marine and terrestrial sources around the world to build an extensive library of natural chemical compounds with potential disease-fighting capability.

Research Highlight: Red Sea

The Life Sciences Institute's David Sherman explores biochemical pathways of marine microorganisms to find new drug candidates to treat infectious diseases and cancers. To collect the samples he needs for his work, he often trades his lab coat for a wet suit and travels to exotic locations rich in biodiversity resources. In November 2014, Sherman traveled with fellow LSI faculty member and frequent collaborator Georgios Skiniotis, a structural biologist, to Saudi Arabia to collect marine microorganisms from the Red Sea.

Recent Publications

Hansen, D.A., Koch, A.A., Sherman. D.H. 2015. Substrate controlled divergence in polyketide synthase catalysis. J. Am. Chem. Soc. 137(11):3735-3738.

Smith, J.L., Skiniotis, G., Sherman, D.H. 2015. Architecture of the polyketide synthase module: surprises from electron cryo-microscopy. Curr. Opin. Struct. Biol. Review {Epub ahead of print}

Bernard, S.M., Akey, D.L., Triapthi, A., Park S.-R., Konwerski, J.R., Anzai, Y., Li, S., Kato, F., Sherman, D.H., Smith, J.L. 2015. Structural basis of substrate specificity and regiochemistry in the MycF/TylF family of sugar O-methyltransferases. ACS Chem. Biol. {Epub ahead of print}