Eliseu O. De Oliveira profile photo

Eliseu O. De Oliveira

Research Assistant Professor, Medicines for All

Richmond, VA, US

804-828-9069 eodeoliveira@vcu.edu

De Oliveira researches chemical processes for cleaner and more economical routes of synthesis for drugs needed in developing countries









Eliseu O. De Oliveira, M.S., Ph.D., graduated from the University of São Paulo (Ph.D. in medicinal chemistry; M.S. in organic chemistry), followed by postdoctoral fellowships in the U.S. at Virginia Commonwealth University and Georgetown University. His expertise has been applied to the development of methodologies for synthesis of nitrogen containing heterocyclic compounds of biological interest and relevant to the design of chemical manufacturing processes. He has successfully conducted projects with small molecules for drug discovery for respiratory inflammation (LTA4H modulators for COPD), breast cancer (BRCA1 mimetics), novel pro-cognitive CNS agents (5-HT7 antagonists) and synthesis of marine natural products for potential analgesic activity (hermitamides A and B).

As an assistant professor in VCU's Medicines for All program, he researches novel chemical processes for cleaner and more economical routes of synthesis for drugs greatly needed in developing countries (e.g. Dolutegravir for AIDS/HIV). Before coming to VCU, De Oliveira served as the scientific coordinator of the Georgetown University Center for Drug Discovery in the Chemical Biology Consortium of the National Cancer Institute's Next Therapeutics Program. He is also Co-Founder of the Brazilian Expert Network (BEN), a non-profit organization focused on bridging the innovation gap between Brazil and the U.S.

Industry Expertise

  • Biotechnology
  • Chemicals
  • Education/Learning
  • Pharmaceuticals
  • Research

Areas of Expertise

Drug DiscoveryOrganic ChemistryBiochemistryMolecular BiologyProtein PurificationMedicinal Chemistry


Universidade de São Paulo

PhD, Medicinal Chemistry


Selected Articles

BRCA1-mimetic compound NSC35446. HCl inhibits IKKB expression by reducing estrogen receptor-α occupancy in the IKKB promoter and inhibits NF-κB activity in antiestrogen-resistant human breast cancer.. | Breast cancer research and treatment


We previously identified small molecules that fit into a BRCA1-binding pocket within estrogen receptor-alpha (ERα), mimic the ability of BRCA1 to inhibit ERα activity (“BRCA1-mimetics”), and overcome antiestrogen resistance. One such compound, the hydrochloride salt of NSC35446 (“NSC35446.HCl”), also inhibited the growth of antiestrogen-resistant LCC9 tumor xenografts. The purpose of this study was to investigate the downstream effects of NSC35446.HCl and its mechanism of action.

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A new class of small molecule estrogen receptor-alpha antagonists that overcome anti-estrogen resistance | Oncotarget


Previous studies indicate that BRCA1 protein binds to estrogen receptor-alpha (ER) and inhibits its activity. Here, we found that BRCA1 over-expression not only inhibits ER activity in anti-estrogen-resistant LCC9 cells but also partially restores their sensitivity to Tamoxifen. To simulate the mechanism of BRCA1 inhibition of ER in the setting of Tamoxifen resistance, we created a three-dimensional model of a BRCA1-binding cavity within the ER/Tamoxifen complex; and we screened a pharmacophore database to identify small molecules that could fit into this cavity.

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Effect of the leukotriene A(4) hydrolase aminopeptidase augmentor 4-methoxydiphenylmethane in a pre-clinical model of pulmonary emphysema | Bioorganic & medicinal chemistry letters


The leukotriene A(4) hydrolase enzyme is a dual functioning enzyme with the following two catalytic activities: an epoxide hydrolase function that transforms the lipid metabolite leukotriene A(4) to leukotriene B(4) and an aminopeptidase function that hydrolyzes short peptides. To date, all drug discovery efforts have focused on the epoxide hydrolase activity of the enzyme, because of extensive biological characterization of the pro-inflammatory properties of its metabolite, leukotriene B(4). Herein, we have designed a small molecule, 4-methoxydiphenylmethane, as a pharmacological agent that is bioavailable and augments the aminopeptidase activity of the leukotriene A(4) hydrolase enzyme.

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Synthesis and evaluation of hermitamides A and B as human voltage-gated sodium channel blockers | Bioorganic & medicinal chemistry


Hermitamides A and B are lipopeptides isolated from a Papau New Guinea collection of the marine cyanobacterium Lyngbya majuscula. We hypothesized that the hermitamides are ligands for the human voltage-gated sodium channel (hNa(V)) based on their structural similarity to the jamaicamides. Herein, we describe the nonracemic total synthesis of hermitamides A and B and their epimers. We report the ability of the hermitamides to displace [(3)H]-BTX at 10 μM more potently than phenytoin, a clinically used sodium channel blocker.

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