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Andrew G. Cheetham

Researcher at Johns Hopkins University

Publications -  43
Citations -  3637

Andrew G. Cheetham is an academic researcher from Johns Hopkins University. The author has contributed to research in topics: Drug delivery & Prodrug. The author has an hindex of 28, co-authored 39 publications receiving 3116 citations. Previous affiliations of Andrew G. Cheetham include Northwestern University & University of Oxford.

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Supramolecular Nanostructures Formed by Anticancer Drug Assembly

TL;DR: This strategy to directly assemble the small molecular hydrophobic anticancer drug camptothecin into discrete, stable, well-defined nanostructures with a high and quantitative drug loading presents new opportunities for the development of self-delivering drugs for cancer therapeutics.
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Self-assembly of giant peptide nanobelts.

TL;DR: The sequences for these molecules that can eliminate all curvature from the nanostructures they form in water and generate completely flat nanobelts with giant dimensions relative to previously reported systems are discovered.
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Peptide-drug conjugates as effective prodrug strategies for targeted delivery.

TL;DR: The recent progress in the design and synthesis of self‐assembling peptide‐drug amphiphiles to construct supramolecular nanomedicine and nanofiber hydrogels for both systemic and topical delivery of active pharmaceutical ingredients is highlighted.
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Amino acid sequence in constitutionally isomeric tetrapeptide amphiphiles dictates architecture of one-dimensional nanostructures.

TL;DR: The use of isomeric peptide amphiphiles as molecular building blocks to create one-dimensional (1D) nanostructures is reported to demonstrate the significance of peptide side chain interactions in determining the architectures of supramolecular assemblies.
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Self-Assembled Tat Nanofibers as Effective Drug Carrier and Transporter

TL;DR: Fluorescence and confocal microscopy imaging show that the Tat nanofibers can effectively transport encapsulated molecules into the cells through an adsorptive-mediated endocytosis pathway, and Cytotoxicity experiments and flow cytometry measurements demonstrate that PTX loaded in the nan ofibers exerts its cytotoxicity against cancer cells by arresting the cells at the G2/M phase, the same working mechanism as free PTX.