{"entity": "researcher", "timestamp": "2026-08-28T00:12:00.764Z", "family": "Ferreira", "given": "Ricardo J", "initials": "RJ", "orcid": "0000-0003-2590-8229", "affiliations": ["Science for Life Laboratory, Department of Cell and Molecular Biology , Uppsala University , Box 596, 75124 Uppsala , Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/e914a4abf07c44d8b110d598337f5c54.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/e914a4abf07c44d8b110d598337f5c54"}}, "publications": [{"entity": "publication", "iuid": "415292e4b69147b9b276029f2e02da3b", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/415292e4b69147b9b276029f2e02da3b.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/415292e4b69147b9b276029f2e02da3b"}}, "title": "Theoretical studies on 1,4-dihydropyridine derivatives as P-glycoprotein allosteric inhibitors: insights on symmetry and stereochemistry.", "authors": [{"family": "Mollazadeh", "given": "Shirin", "initials": "S"}, {"family": "Hadizadeh", "given": "Farzin", "initials": "F", "orcid": "0000-0002-7680-8191", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/705de66c147e409792f22402645c7cca.json"}}, {"family": "Ferreira", "given": "Ricardo J", "initials": "RJ", "orcid": "0000-0003-2590-8229", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e914a4abf07c44d8b110d598337f5c54.json"}}], "type": "journal article", "published": "2021-08-00", "journal": {"title": "J Biomol Struct Dyn", "issn": "1538-0254", "volume": "39", "issue": "13", "pages": "4752-4763", "issn-l": null}, "abstract": "P-glycoprotein (P-gp) is a key efflux pump involved in cellular multidrug resistance (MDR), lowering the concentration of many anticancer drugs in tumor cells by pumping them into the extracellular milieu. While previous studies identified 1,4-dihydropyridines (DHP) as putative P-gp allosteric inhibitors, none reported the effect of stereochemistry on the ability of DHPs to bind P-gp. In the present study both symmetric (1) and asymmetric (2 R,S) DHPs were designed as P-gp inhibitors and, after biological evaluation, molecular docking and molecular dynamics simulation (MD) studies were performed to gain insights on how both scaffolds interact with P-gp. The results were thoroughly analyzed i) to evaluate the role of the different substituents and ii) to assess how stereochemistry may affect binding of DHPs to P-gp. Our results suggest that both the substitution pattern and stereochemistry may have a significant impact not only in drug binding but also on membrane permeation/accumulation, thus compromising in which site the DHPs may exert their effect as P-gp efflux inhibitors. Therefore, it is our conclusion that the stereochemistry cannot be neglected during the development of novel 1,4-dihydropyridine derivatives.Communicated by Ramaswamy H. Sarma.", "doi": "10.1080/07391102.2020.1780942", "pmid": "32573349", "labels": [], "xrefs": [], "notes": [], "created": "2026-08-21T12:04:43.183Z", "modified": "2026-08-21T12:04:43.317Z"}, {"entity": "publication", "iuid": "285621f1c6ce4a16b86fb87b67a5f7cc", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/285621f1c6ce4a16b86fb87b67a5f7cc.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/285621f1c6ce4a16b86fb87b67a5f7cc"}}, "title": "Antibiotic Uptake Across Gram-Negative Outer Membranes: Better Predictions Towards Better Antibiotics.", "authors": [{"family": "Ferreira", "given": "Ricardo J", "initials": "RJ", "orcid": "0000-0003-2590-8229", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e914a4abf07c44d8b110d598337f5c54.json"}}, {"family": "Kasson", "given": "Peter M", "initials": "PM", "orcid": "0000-0002-3111-8103", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/8c30532fab22425ab83ea04a65e33f72.json"}}], "type": "journal article", "published": "2019-12-13", "journal": {"title": "ACS Infect Dis", "issn": "2373-8227", "volume": "5", "issue": "12", "pages": "2096-2104", "issn-l": "2373-8227"}, "abstract": "Crossing the Gram-negative bacterial membrane poses a major barrier to antibiotic development, as many small molecules that can biochemically inhibit key bacterial processes are rendered microbiologically ineffective by their poor cellular uptake. The outer membrane is the major permeability barrier for many drug-like molecules, and the chemical properties that enable efficient uptake into mammalian cells fail to predict bacterial uptake. We have developed a computational method for accurate prospective prediction of outer membrane uptake of drug-like molecules, which we combine with a new medium-throughput experimental assay of outer membrane vesicle swelling. Parallel molecular dynamics simulations of compound uptake through Escherichia coli (E. coli) OmpF are used to successfully and quantitatively predict experimental permeabilities measured via either outer membrane swelling or prior liposome-swelling measurements. These simulations are analyzed using an inhomogeneous solubility-diffusion model to yield predictions of permeability. For most polar molecules we test, outer membrane permeability also correlates well with whole-cell uptake. The ability to accurately predict and measure outer membrane uptake of a wide variety of small molecules will enable simpler determination of which molecular scaffolds and which derivatives are most promising prior to extensive chemical synthesis. It will also assist in formulating a more systematic understanding of the chemical determinants of outer membrane permeability.", "doi": "10.1021/acsinfecdis.9b00201", "pmid": "31593635", "labels": [], "xrefs": [], "notes": [], "created": "2026-08-21T11:36:24.151Z", "modified": "2026-08-21T11:36:24.248Z"}]}