Bio

Academic Appointments


Honors & Awards


  • Herman Lopata Postdoctoral Hepatitis Research Fellowship, American Liver Foundation (2010-2011)
  • Dean's Fellowship, Stern Fund (2010)

Professional Education


  • GME, University of Washington Seattle, Internal Medicine Residency (2008)

Research & Scholarship

Current Research and Scholarly Interests


Hepatitis C virology, bio-organic chemistry, and chemical biology. My current work focuses on probing the interaction between the NS5A nonstructural protein of HCV and PIP2, a membrane lipid found in all cells. Disruption of this interaction appears to prevent HCV from replicating.

Publications

Journal Articles


  • Mixing the right hepatitis C inhibitor cocktail TRENDS IN MOLECULAR MEDICINE Gelman, M. A., Glenn, J. S. 2011; 17 (1): 34-46
  • Biocidal activity of polystyrenes that are cationic by virtue of protonation ORGANIC LETTERS Gelman, M. A., Weisblum, B., Lynn, D. M., GELLMAN, S. H. 2004; 6 (4): 557-560

    Abstract

    [structure: see text] Poly(1) kills bacteria (Gram-positive and -negative) and lyses human erythrocytes; this biocidal profile is similar to that of the peptide toxin mellitin. Poly(1) has antibacterial activity comparable to that of a potent derivative of the host defense peptide magainin II, but lacks magainin's selectivity for bacteria over erythrocytes. An analogous N-quaternized polymer, poly(3), is less biocidal than poly(1), suggesting that reversible N-protonation leads to greater biocidal activity than does irreversible N-quaternization.

    View details for DOI 10.1021/ol036341+

    View details for Web of Science ID 000188926400026

    View details for PubMedID 14961622

  • Selective binding of TAR RNA by a tat-derived beta-peptide ORGANIC LETTERS Gelman, M. A., Richter, S., Cao, H., Umezawa, N., GELLMAN, S. H., Rana, T. M. 2003; 5 (20): 3563-3565

    Abstract

    [structure: see text] The interaction between the HIV-1 Tat protein and the TAR RNA element in the nascent viral genomic transcript is required for viral replication. An 11-residue beta-peptide (1), an all-beta homologue of the Arg-rich region Tat 47-57, binds TAR RNA with K(d) = 29 +/- 4 nM. A control beta-peptide (2) in which all Arg side chains are replaced by Lys side chains shows increased affinity but decreased specificity for wild-type vs bulge-deleted TAR RNA, as do the alpha-peptide analogues of 1 and 2.

    View details for DOI 10.1021/ol034977v

    View details for Web of Science ID 000185565500005

    View details for PubMedID 14507173

  • Translocation of a beta-peptide across cell membranes JOURNAL OF THE AMERICAN CHEMICAL SOCIETY Umezawa, N., Gelman, M. A., Haigis, M. C., Raines, R. T., Gellman, S. H. 2002; 124 (3): 368-369

    Abstract

    Short cationic peptides derived from DNA-binding proteins, of which HIV Tat is a prototype, can cross the membranes of living cells, and they can bring covalently attached moieties (proteins, drugs) along with them. We show that a beta-amino acid analogue of Tat 47-57 enters HeLa cells with comparable efficiency to Tat 47-57 itself (YGRKKRRQRRR). The beta-peptide is comprised of residues that bear the appropriate side chain at the beta-carbon. Both the alpha- and the beta-peptide were conjugated to fluorescein at the N terminus, and cell penetration was monitored by confocal fluorescence microscopy. Deletion of the three C-terminal arginine residues from the alpha-peptide abolished translocation activity, consistent with prior reports, and deletion of the three C-terminal beta3-homoarginine residues from the beta-peptide had a similarly adverse effect. Thus, alpha- and beta-peptide translocation processes show similar length/charge dependence. The beta-peptide appeared to be largely unfolded in water, which is consistent with the behavior of short Tat-derived alpha-peptides, but in methanol the beta-peptide adopted a helical conformation, in contrast to short Tat-derived alpha-peptides. Our results show that neither altering the oligomeric backbone (amide group spacing) nor increasing the intrinsic propensity to adopt a specific secondary structure affects translocation activity.

    View details for DOI 10.1021/ja017283v

    View details for Web of Science ID 000173356900002

    View details for PubMedID 11792194

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