Faculty

Nicole S. SampsonNicole S. Sampson, Professor and Chair

B.S. Harvey Mudd College, 1985
Ph.D. University of California, Berkeley, 1990
American Cancer Society Postdoctoral Fellowship, Harvard University, 1991-1993

659 Chemistry
Phone: (631) 632-7952 | Fax: (631) 632-5731
Email:

The Sampson Group Website

Positions

Member of Graduate Programs in: Chemistry, Biochemistry & Structural Biology, Molecular & Cellular Pharmacology

Co-Director Chemical Biology Training Program

Member of Institute of Chemical Biology and Drug Discovery

Chair, Department of Chemistry

Chemical Biology, Enzymology & Metabolomics

The research in our laboratory focuses on understanding the relationship between protein structure and protein function and synthesizing chemical tools to probe and control biological function. Work is ongoing in five different areas:

  • AROMP
    Cancer Metastasis
    Lipid-Protein Interactions
    Mammalian Fertilization
    Tuberculosis Steroid Metabolism

Awards/Honors

  • Camille and Henry Dreyfus Foundation New Faculty Award, 1993-1998
  • National Science Foundation Career Award, 1996-2000
  • American Chemical Society Arthur C. Cope Scholar Award, 2001
  • American Chemical Society Pfizer Award in Enzyme Chemistry, 2005
  • Research Foundation of SUNY Research and Scholarship Award, 2005

Publications

  1. Romoff, T. T.; Sampson, N. S.; van Eikeren, P., (1987) “Regioselectivity and Kinetics of Hydride Transfer in Substituted 1-Benzyl-3-quinoline¬carboxamide Redox Reactions,” J. Org. Chem. 52, 4454-4459.
  2. Sampson, N. S.; Bartlett, P. A., (1988) “Synthesis of Phosphonic Acid Derivatives by Oxidative Activation of Phosphinate Esters,” J. Org. Chem. 53, 4500-4503.
  3. Bartlett, P. A.; Sampson, N. S.; Reich, S. H.; Drewry, D. H.; Lamden, L. A., (1990) “The Interplay Between Enzyme Mechanism, Protein Structure, and the Design of Serine Protease Inhibitors,” in Gregg, V. A. ed., The Use of X-ray Crystallography in the Design of Antiviral Agents, Associated Press, 247-259.
  4. Sampson, N. S.; Bartlett, P. A., (1991) “Peptidic Phosphonylating Agents as Irreversible Inhibitors of Serine Proteases and Models of the Tetrahedral Intermediates,” Biochemistry 30, 2255-2263.
  5. Bone, R.; Sampson, N. S.; Bartlett, P. A.; Agard, D. A., (1991) “Crystal Structures of a-Lytic Protease Complexes with Irreversibly Bound Phosphonate Esters,” Biochemistry 30, 2263-2272.
  6. Sampson, N. S.; Bartlett, P. A., (1991) “Attempted de Novo Design, Synthesis, and Evaluation of a Ligand for the Allosteric Site of Phosphofructokinase,” J. Org. Chem. 56, 7179-7183.
  7. Sampson, N. S.; Knowles, J. R., (1992) “Segmental Movement: Definition of the Structural Requirements for Loop Closure in Catalysis by Triosephosphate Isomerase,” Biochemistry, 31, 8482-8487.
  8. Sampson, N. S.; Knowles, J. R., (1992) “Segmental Motion in Catalysis: Investi¬gation of a Critical Hydrogen Bond for Loop Closure in the Reaction of Triose¬phosphate Isomerase,” Biochemistry, 31, 8488-8494.
  9. Kass, I. J.; Sampson, N. S., (1995) “The Isomerization Catalyzed by Brevibacterium sterolicum Cholesterol Oxidase Proceeds Stereospecifically with One Base,” Biochem. Biophys. Res. Commun., 206, 688-693.
  10. Sampson, N. S., (1996) Review of "Understanding Enzymes", 4th Ed., by Trevor Palmer, Quart. Rev. Biol., 71, 116. – Book review
  11. Sun, J. and Sampson, N. S., (1997) Review of “Short Protocols in Molecular Biology. A Compendium of Methods from Current Protocols in Molecular Biology,” 3rd ed., Ausubel, F. M.; Brent, R.; Kingston, R. E.; Moore, D. D.; Seidman, J. G. Smith, J. A.; Struhl, K., eds., Quart. Rev. Biol., 72, 71. – Book review
  12. Chen, X. and Sampson, N.S., (1997) Review of “Contemporary Enzyme Kinetics and Mechanism,” 2nd ed., Parich, D. L., eds., Quart. Rev. Biol., 72, 320. – Book review
  13. Sampson, N. S.; Kass, I. J., (1997) “Isomerization but not Oxidation is Suppressed by a Single Point Mutation, E361Q, in the Reaction Catalyzed by Cholesterol Oxidase,” J. Am. Chem. Soc., 119, 855-862.
  14. Ghoshroy, K. B.; Zhu, W.; Sampson, N. S., (1997) "Investigation of Membrane Disruption in the Reaction Catalyzed by Cholesterol Oxidase," Biochemistry, 36, 6133-6140.
  15. Pyluck, A.; Ruiyong, Y.; Galligan Jr, E.; Primakoff, P.; Myles, D. G.; Sampson, N. S., (1997) “ECD Peptides Inhibit In Vitro Fertilization in Mice,” Bioorg. Med. Chem. Lett., 7, 1053-1058.
  16. Sampson, N. S.; McCann, A. E., (1997) "4,5-Cyclopropano-Cholestan-3b-Ol Substrates for Cholesterol Oxidase and Their 1H NMR Assignments, " J. Org. Chem., 62, 5893 -5897.
  17. Sampson, N. S.; Chen, X., (1998) “Improved Expression of Brevibacterium sterolicum Cholesterol Oxidase in Escherichia coli by Genetic Modification,” Prot. Exp. Purific., 12, 347-352.
  18. Sampson, N. S.; Kass, I. J.; Ghoshroy, K. B., (1998) “A Truncated Ω Loop Mutant of Cholesterol Oxidase Has Altered Substrate Specificity,” Biochemistry, 37, 5770-5778.
  19. Sun, J.; Sampson, N. S., (1998) “Determination of the Amino Acid Requirements for a Protein Hinge in Triosephosphate Isomerase,” Prot. Science, 7, 1495-1505. PMC2144049
  20. Chen, H.; Pyluck, A.; Janik, M.; Sampson, N. S., (1998) “Peptides Corresponding to the Epidermal Growth Factor-like Domain of Mouse Fertilin: Synthesis and Biological Activity,” Biopolymers (Peptide Science), 47, 299-307.
  21. Kass, I. J.; Sampson, N. S., (1998) “The Importance of Glu361 Position in the Reaction Catalyzed by Cholesterol Oxidase,” Bioorg. Med. Chem. Lett., 8, 2663-2668.
  22. Kass, I. J.; Sampson, N. S., (1998) “Evaluation of the Role of His447 in the Reaction Catalyzed by Cholesterol Oxidase,” Biochemistry, 37, 17990-18000.
  23. Chen, H.; Sampson, N.S., (1999) “Mediation of Mammalian Sperm-Egg Fusion: Evidence That Mouse Egg α6β1 Integrin is the Receptor for Sperm Fertilinβ,” Chem. Biol., 6, 1-10.
  24. Yue, Q. K.; Kass, I. J.; Sampson, N. S.; Vrielink, A., (1999) “Crystal Structure Determination of Cholesterol Oxidase from Streptomyces and Structural Characterization of Key Active Site Mutants,” Biochemistry, 38, 4277-4286.
  25. Sun, J.; Sampson, N. S., (1999) “Understanding Protein Lids: Kinetic Analysis of Active Hinge Mutants in Triosephosphate Isomerase,” Biochemistry, 38, 11474-11481.
  26. Gupta, S.; Li, H.; Sampson, N. S., (2000) “Characterization of Fertilinβ-Disintegrin Binding Specificity in Sperm-Egg Adhesion,” Bioorg. Med. Chem., 8, 723-729.
  27. McCann, A.; Sampson, N. S., (2000) “A C6-FAD Adduct is Formed Upon Irreversible Inactivation of Cholesterol Oxidase by 2α,3α-Cyclopropano-5α-cholestan-3β-ol,” J. Am. Chem. Soc., 122, 35-39.
  28. Chen, X.; Wolfgang, D.; Sampson, N. S., (2000) "Use of the Parallax-Quench Method to Determine the Position of the Active-Site Loop of Cholesterol Oxidase in Lipid Bilayers," Biochemistry, 39, 13383-13389.
  29. Xiang, J; Sun, J.; Sampson, N. S. (2001) "The Importance of Hinge Sequence for Loop Function and Catalytic Activity in the Reaction Catalyzed by Triosephosphate Isomerase," J. Mol. Biol, 307, 1103-1112.
  30. Sampson, N. S.; Sarah T. Ryan; Deborah A. Enke; Dominic Cosgrove; Victor Koteliansky; Philip Gotwals (2001) "Global Gene Expression Analysis Reveals a Role for the α1 Integrin in Renal Pathogenesis," J. Biol. Chem, 276, 34182-34188.
  31. Sampson, N. S. (2001) "Dissection of a Flavo-Enzyme Active Site: the Reaction Catalyzed by Cholesterol Oxidase," Antioxidants and Redox Signalling, 3, 839-846. – Invited Review
  32. Ye, Y,; Lario, P. Vrielink, A.; Sampson, N. S. (2001) "Structural and Kinetic Analysis of the Role of Asn485 in the Reaction Catalyzed by Cholesterol Oxidase," Biochemistry, 40, 13779-13787.
  33. Sampson, N. S. (2001) "The Emerging Global Paradigm for Scientific Research," in New Voices in Chemistry, Chem. Eng. News, 26 Mar 2001, 187. – Essay
  34. Gupta, S.; Sampson, N. S. (2001) "Dimyristoylated Peptides Incorporated into Liposomes Are Polyvalent Fertilinβ Mimics," Org. Lett. 3, 3333-3335.
  35. Sampson, N.S.; Mrksich, M.; Bertozzi, C.R. (2001) "Surface Molecular Recognition," Proc. Nat. Acad. Sci. U.S.A. 98, 12870-12871. PMC60788 – Essay
  36. Li, H.; Sampson, N. S. (2002) "Structural Analysis of Cyclic Peptide Fertilinβ Mimics That Are Ligands for α6β1 Integrin," J. Pep. Res. 59, 49-54.
  37. Ye, Y,; Liu, Pingsheng; Anderson, R.; Sampson, N. S. (2002) "Construction of a Catalytically Inactive Cholesterol Oxidase Mutant: Investigation of the Interplay Between Active Site Residues Glutamate 361 and Histidine 447," Arch. Biochem Biophys. 402, 235-242.
  38. Roberts, S.K.; Sampson, N. S. (2003) “Increased Polymer Length of Oligopeptide-substituted Polynorbornenes using LiCl,” J. Org. Chem. 68, 2020-2023.
  39. Lario, P.; Sampson, N.S.; Vrielink, A. (2003) “Sub-Atomic Resolution Crystal Structure of Cholesterol Oxidase: What Atomic Resolution Crystallography Reveals About Enzyme Mechanism and the Role of the FAD Cofactor In Redox Activity,” J. Mol. Biol. 326 1635-1650.
  40. Roberts, S. K.; Konkar, S.; Sampson, N. S. (2003) “Comparison of Fertilinβ Peptide-Substituted Polymers and Liposomes as Inhibitors of In Vitro Fertilization,” ChemBioChem 4, 1229-1231.
  41. Sampson, N. S.; Vrielink, A. (2003) “Cholesterol Oxidases: A Study of Nature’s Approach to Protein Design,” Acc. Chem. Res. 36, 713-722. – Invited Review
  42. Kempf, J. G.; Jung, J-y.; Sampson, N. S.; Loria, J. P. (2003) Off-Resonance TROSY (R1p-R1) for Quantitation of Fast Exchange Processes in Large Proteins,” J. Am. Chem. Soc. 125, 12064-12065.
  43. Vrielink, A.; Sampson, N. S.; (2003) “Sub-Ångstrom Resolution Protein Structures: Is Seeing Believing?,” Curr. Opin. Struct. Biol. 13 709-713. – Invited Review
  44. Ahn, K-w.; Sampson, N. S. (2004) “Cholesterol Oxidase Senses Subtle Changes in Lipid Bilayer Structure,” Biochemistry 43, 827-836.
  45. Konkar, S.; Gupta, S.; Sampson, N. S. (2004) “Fertilinβ Liposomes Inhibit In Vitro Fertilization by Steric Blockage,” Bioorg. Med. Chem. Lett. 4, 1381-1384. part of a Symposium-In-Print on “Therapeutic Intervention Targeting Protein-Protein Interactions”.
  46. Xiang, J.; Sampson, N. S. (2004) "Library Screening Studies to Investigate Substrate Specificity in the Reaction Catalyzed by Cholesterol Oxidase," Prot. Engineering, Design & Selection, 17, 341-348.
  47. Xiang, J.; Jung, J-y.; Sampson, N. S. (2004) “Entropy Effects on Protein Hinges: the Reaction Catalyzed by Triosephosphate Isomerase,” Biochemistry, 43, 11436-11445.
  48. Kursula, I.; Salin, M.; Sun, J.; Borledge, B.; Haapalainen, A.; Sampson, N. S.; Wierenga, R. K. (2004) "Understanding Protein Lids: Structural Analysis of Active Hinge Mutants in Triosephosphate Isomerase," Prot. Engineering, Design & Selection, 17, 375-382.
  49. Roberts, K. S.; Sampson, N. S. (2004) “A Facile Synthetic Route Leading to Fluorescently Labeled ROMP Polymers,” Org. Lett. 6, 3253-3255.
  50. Baessler, K.; Lee, Y.; Roberts, K. S.; Facompre, N.; Sampson, N. S. (2006) “Multivalent fertilinβ oligopeptides: the dependence of fertilization inhibition on length and density,” Chem. Biol. 13, 251-259. PMC1475738
  51. Lee, J; Parker, K. L.; Sampson, N. S. (2006) “Amino Acid-Bearing ROMP polymers with a Stereoregular Backbone,” J. Am. Chem. Soc. 128, 4578-4579. PMC2562595
  52. Lee, Y.; Sampson, N. S.; (2006) “ROMPing the Cellular Landscape: Linear Scaffolds for Molecular Recognition,” Curr. Opin. Struct. Biol. 16, 544-550. – Invited Review
  53. Lee, Y.; Baessler, K.; Sampson, N. S. (2006) “ROMP of norbornyl oligopeptides: A versatile synthetic method for exploring receptor topology,” in Understanding Biology Using Peptides, S. Blondelle, ed., American Peptide Society (2005), 59-60.
  54. Kempf, J. G.; Jung, J-y.; Ragain, C.; Sampson, N. S.; Loria, J. P. (2007) “Dynamic requirements for a functional protein hinge,” J. Mol. Biol. 368, 131-149. PMC2203303
  55. Nesbitt, N. M.; Sampson, N.S. (2007) “Antifungal Tradecraft by Cholesterol Oxidase,” Chem. Biol. 14, 238-241. – Preview
  56. Yang, X; Dubnau, E. Smith, I; Sampson, N. S. (2007) “Rv1106c from Mycobacterium tuberculosis is a 3β-hydroxysteroid dehydrogenase,” Biochemistry, 46, 9058-9067. PMC2596615
  57. Lyubimov, A. Y.; Heard, K. Tang, H.; Sampson, N. S; Vrielink, A. (2007) “Distortion of flavin geometry linked to ligand binding in cholesterol oxidase,” Protein Science, 16, 2647-2656. PMC2222809
  58. Sampson, N. S. and Kwak, S. (2008) “ Catalysis at the membrane Interface: Cholesterol oxidase as a case study“, in Proceedings of the 3rd International Beilstein Workshop on Experimental Standard Conditions of Enzyme Characterizations. Beilstein, Germany.
  59. Chen, L.; Lyubimov, A. Y.; Vrielink, A.; Sampson, N. S. (2008) “The binding and release of oxygen and hydrogen peroxide are directed by a hydrophobic tunnel in cholesterol oxidase,” Biochemistry, 47, 5368–5377. PMC66763
  60. Elalami, A; Baessler, K.; Kong, F.; Sampson, N. S.; Kreit, J. (2008) “Subcellular forms of cholesterol oxidase from Rhodococcus sp. CIP 105 335: induction, solubilization and characterization,” in Current Research Topics in Applied Microbiology and Microbial Biotechnology, World Scientific Publishing. Editor: Antonio Mendez-Vilas. Pages 729-735. ISBN-13: 978-981-283-754-7
  61. Dufour, A.; Sampson, N. S.; Zucker, S.; Cao, J. (2008) “Role of the hemopexin domain of matrix metalloproteinase-9 in cell migration,” J. Cell Physiol., 217, 643-651. PMC2574584
  62. Lee, Y.; Sampson, N. S. (2009) “Polymeric ADAM protein mimics interrogate mammalian sperm-egg binding,” ChemBioChem, 10, 929-937. PMC2742739
  63. Song, A.; Parker, K. A.; Sampson, N. S. (2009) “Synthesis of copolymers by alternating romp (AROMP),” J. Am. Chem. Soc., 131, 3444–3445. PMC2718539
  64. Baessler, K.; Lee, Y.; Sampson, N. S. (2009) “β1 Integrin is an adhesion protein for sperm binding to eggs,” ACS Chem. Biology, 4, 357-366. PMC2683199 [non-subscribers] [subscribers]
  65. Yang, X.; Nesbitt, N. M.; Dubnau, E.; Smith, I.; Sampson, N. S. (2009), “Cholesterol metabolism increases the metabolic pool of propionate in M. tuberculosis,” Biochemistry, 48, 3819–3821. PMC2771735 [non-subscribers] [subscribers]
  66. Kreit, J; Sampson, N. S. (2009) “Cholesterol oxidase: Physiological functions,” FEBS, 276, 6844-6856. PMC2805774. – Invited Review. [abstract]
  67. Lyubimov, A. Y.; Chen, L.; Sampson, N. S.; Vrielink, A. (2009) “A hydrogen-bonding network is important for oxidation and isomerization in the reaction catalyzed by cholesterol oxidase,” Acta Crys. D, 65, 1222-1231. PMC3089011.
  68. Nesbitt, N. M.; Fontán, P.; Kolesnikova, I.; Smith, I.; Sampson, N. S.; Dubnau, E. (2010) “A thiolase of M. tuberculosis is required for virulence and for production of androstenedione and androstadienedione from cholesterol,” Infect. Immun., 78, 275-282. PMC2798224
  69. Dufour, A.; Sampson, N. S.; Kuscu, C.; Zucker, S.; Cao, J. (2010) “Role of MMP-9 dimers in cell migration: design of inhibitor peptides,” J. Biol. Chem., 285, 35944-35956. 10.1074/jbc.M109.091769. PMC2975217. [link]
  70. Song, A.; Lee, J.; Parker, K. A.; Sampson, N. S. (2010) “Scope of the ring opening metathesis polymerization (ROMP) reaction of 1-substituted cyclobutenes,” J. Am. Chem. Soc., 132, 10513–10520. 10.1021/ja1037098. PMC2718539. http://pubs.acs.org/doi/full/10.1021/ja1037098
  71. Song, A.; Parker, K. A.; Sampson, N. S. (2010) “Cyclic alternating ROMP (CAROMP). Rapid access to functionalized cyclic polymers,” Org. Lett., 12, 3729-3731. 10.1021/ol101432m. PMC2933648. [link]
  72. Yang, X.; Gao, J.; Smith, I.; Dubnau, E.; Sampson, N. S. (2011), “Cholesterol is not an essential source of nutrition for Mycobacterium tuberculosis during infection,” J. Bact., 193, 1473-1476. 10.1128/JB.01210-10. PMC3067635
  73. Song, A.; Walker, S. G.; Parker, K. A.; Sampson, N. S. (2011) “Antibacterial studies of alternating, random and homo-polymers with varied positions of cationic side chains,” ACS Chem. Biol., 6, 590-599. doi: 10.1021/cb100413w PMC3117943
  74. Thomas, S.; Yang, X.; Sampson, N. S. (2011), “Inhibition of the M. tuberculosis 3β-hydroxysteroid dehydrogenase by azasteroids,” Bioorg. Med. Chem. Lett., 21, 2216-2219. 10.1016/j.bmcl.2011.03.004 PMC3077731
  75. Dufour, A.; Sampson, N. S.; Rizzo, R; DeLeon, J; Li, J; Kuscu, C.; Zhi, J.; Jaber, N.; Liu, E.; Zucker, S.; Cao, J. (2011) “Small molecule anti-cancer therapy selectively targets the hemopexin domain of matrix metalloproteinase-9 (MMP-9),” Cancer Res., 71, 4977-4988. 10.1158/0008-5472 PMC3138841
  76. Zarrabi, K.; Dufour, A.; Li, J; Kuscu, C.; Kozarekar, P.; Zhi, J.; Sampson, N. S.; Zucker, S.; Cao, J. (2011) “Inhibition of matrix metalloproteinase-14 (MMP-14)-mediated cancer cell migration,” J. Biol. Chem., 286, 38, 33167-77. DOI: http://dx.doi.org/10.1074/jbc.M111.256644
  77. Thomas, S.T., VanderVen, B.C., Sherman, D.R., Russell, D.G., Sampson, N.S. “Pathway profiling in Mycobacterium tuberculosis: elucidation of cholesterol-derived catabolite and enzymes that catalyze its metabolism,” J. Biol. Chem, (2011), 286, 51, 43668-78. DOI: 10.1074/jbc.M111.313643
  78. Ueki, N. Lee, S. Sampson, N. S., Hayman, M. J. (2013) “Selective cancer targeting with prodrugs activated by histone deacetylase and tumour-associated protease,” Nature Comm., 4, 2735-2742. DOI: 10.1038/ncomms3735 
  79. Slayden, R.A., Jackson, M., Zucker, J., Ramirez, M.V., Dawson, C.C., Crew, R., Sampson, N.S., Thomas, S.T., Jamshidi, N., Sisk, P., Caspi, R., Crick, D.C., McNeil, M.R., Pavelka, M.S., Niederweis, M., Siroy, A., Dona, V., McFadden, J., Boshoff, H., Lew, J.M. (2013) “Updating and curating metabolic pathways of TB,” Tuberculosis, 93, 1, 47-59. DOI: 10.1016/j.tube.2012.11.001
  80. Thomas, S.T., Sampson, N.S. “Mycobacterium tuberculosis utilizes a unique heterotetrameric structure for dehydrogenation of the cholesterol side chain,” Biochemistry, (2013), 52, 17, 2895-904. DOI:  10.1021/bi4002979
  81. Evensen N.A., Li J., Yang J., Yu X., Sampson N.S., Zucker, S., Cao, J. (2013) “Development of A High-throughput Screening Invasion Assay for Anti-Cancer Drug Discovery,” PLoS One, 8(12): e82811. DOI: 10.1371/journal.pone.0082811
  82. Wu, L., and Sampson, N. S. (2014) “Fucose, Mannose and β-N-Acetylglucosamine Glycopoly-mers Initiate the Mouse Sperm Acrosome Reaction Through Convergent Signaling Pathways,” ACS Chem. Biol. 9, 468-475 DOI: 10.1021/cb400550j
  83. Gao, J. and Sampson, N. S. (2014) “A GMC Oxidoreductase Homolog is Required for Acetylation of Glycopeptidolipid in Mycobacterium smegmatis,” Biochemistry 53, 611-613 DOI: 10.1021/bi4015083
  84. Wipperman, M., Sampson, N. S., and Thomas, S. T. (2014) “Pathogen “Roid Rage”: Cholesterol Utilization by Mycobacterium tuberculosis,” CRC Critical Reviews in Biochemistry, DOI 10.3109/10409238.2014.895700.
  85. Tan, L., Parker, K., and Sampson, N. S. (2014) “A Bicyclo[4.2.0]octene-derived monomer provides completely linear alternating copolymers via alternating ring-opening metathesis polymerization (AROMP),” Macromolecules DOI: 10.1021/ma5012039 
  86. Yang, M., Guja, K. E., Thomas, S. T., Garcia-Diaz, M. And Sampson, N. S. (2014) “A distinct MaoC-like enoyl-CoA hydratase architecture mediates cholesterol catabolism in Mycobacterium tuberculosis,” ACS Chemical Biology, in press. DOI:10.1021/cb500232h

 

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