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Christopher Cartmell

  • Assistant Research Professor, Pharmacology - (Research Series Track)
  • Member of the Graduate Faculty
Contact
  • (520) 626-6400
  • Life Sciences North, Rm. 567
  • Tucson, AZ 85724
  • cartmell@arizona.edu
  • Bio
  • Interests
  • Courses
  • Scholarly Contributions

Awards

  • Invited Speaker
    • American Society of Pharmacognosy, Fall 2025
  • American Soceity of Pharmacognosy Faculty Starter Award
    • American Society of Pharmacognosy, Spring 2024

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Interests

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Courses

2025-26 Courses

  • Intro to Pharmacology
    PHCL 412 (Fall 2025)
  • Intro to Pharmacology
    PHCL 512 (Fall 2025)

2024-25 Courses

  • Dissertation
    CHEM 920 (Spring 2025)
  • Intro to Pharmacology
    PHCL 412 (Fall 2024)
  • Intro to Pharmacology
    PHCL 512 (Fall 2024)

2023-24 Courses

  • Directed Research
    PHCL 492 (Spring 2024)

Related Links

UA Course Catalog

Scholarly Contributions

Journals/Publications

  • Maw, Z. A., Grunwald, A. L., Haltli, B. A., Cartmell, C., & Kerr, R. G. (2024). Discovery of the Lipopeptides Albubactins A-H from RKJM0023 via Chemical Elicitation with Rhamnolipids and Synthesis of Albubactin A. Journal of natural products, 87(7), 1682-1693.
    More info
    The marine tunicate-derived RKJM0023 was cultured in the presence of a rhamnolipid mixture in an effort to elicit the production of silent natural products. MS/MS-based molecular networking analysis enhanced with nonparametric statistics highlighted the upregulation of a molecular cluster (Kruskal-Wallis = 1.6 e for ) in which no MS/MS features had library matches. Targeted isolation of these features resulted in the discovery of nine new acylated lipopeptides, albubactins A-H (-) each containing a unique glutamine tripeptide and a -terminal ethyl ester moiety. Three related albubactin acids A-C (-) lacking the ethyl ester were also identified. NMR spectroscopy and UPLC-HR-ESI-MS/MS demonstrated that the albubactins were obtained as mixtures that shared a common / and differed only in their acylated terminal groups. Due to the complex spectroscopic elucidation with many overlapping shifts, a total synthesis of albubactin A () was completed and used to determine the absolute configuration of the new albubactins.
  • Maw, Z. A., Haltli, B., Guo, J. J., Baldisseri, D. M., Cartmell, C., & Kerr, R. G. (2024). Discovery of Acyl-Surugamide A2 from Marine RKJM-0023-A New Cyclic Nonribosomal Peptide Containing an N-ε-acetyl-L-lysine Residue. Molecules (Basel, Switzerland), 29(7).
    More info
    We report the discovery of a novel cyclic nonribosomal peptide (NRP), acyl-surugamide A2, from a marine-derived RKJM-0023 (CP133227). The structure of acyl-surugamide A2 was elucidated using a combination of NMR spectroscopy, MS2 fragmentation analysis, and comparative analysis of the biosynthetic gene cluster. Acyl-surugamide A2 contains all eight core amino acids of surugamide A, with a modified N-ε-acetyl-L-lysine residue. Our study highlights the potential of marine strains to produce novel natural products with potential therapeutic applications. The structure of cyclic peptides can be solved using MS2 spectra and analysis of their biosynthetic gene clusters.
  • Cartmell, C. (2023). Investigation of the impact of bacterial microencapsulation on natural product discovery. Current research in Biotechnology.

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