My Science Publications

Over the years, my research career has contributed to publications in the chemistry, biology and nanotech fields. Those publications that are most related to the ideas that inspire the formation of Garden Shed Bionanotech are shown below:

  1. P. Free, C. P. Shaw, R. Lévy; “PEGylation modulates the interfacial kinetics of proteases on peptide-capped gold nanoparticles”, Chem. Commun. 2009, 33, 5009–11. doi: 10.1039/b910657j.
    Summary: my first publication in this area used peptides to cover gold nanoparticles, to be used as a diagnostic tool for protease enzyme activity. The activity was highly dependant on the structure of the peptide layer surrounding the gold nanoparticles.
  2. P. Free*, D. Paramelle, M. Bosman, J. Hobley, D. G. Fernig; “Synthesis of Silver Nanoparticles with Monovalently Functionalized Self-Assembled Monolayers”, Aust. J. Chem. 2012, 65, 275–282. doi: 10.1071/CH11429.
    Summary: similar peptides as above were applied to cover silver nanoparticles. Such particles could be used as alternatives to gold nanoparticles for diagnostic applications, the advantage being an increased sensitivity of silver nanoparticles.
  3. P. Free*, G. Conger, W. Siji, J. B. Zhang, D. G. Fernig; “High colloidal stability of gold nanorods coated with a peptide-ethylene glycol: Analysis by cyanide-mediated etching and nanoparticle tracking analysis”, Colloids Surfaces B 2016, 146, 1–8. doi: 10.1016/j.colsurfb.2016.07.006.
    Summary: highly stable and infrared sensitive gold nanorods were created using peptide coating and a selective etching process.
  4. D. Paramelle, A. Sadovoy, S. Gorelik, P. Free*, J. Hobley, D. G. Fernig; “Rapid method to estimate the concentration of citrate capped silver nanoparticles from UV-visible light spectra”, Analyst 2014, 139, 4855–4861. doi: 10.1039/c4an00978a.
    Summary: publication of the first concise list of absorbance-related characteristics to allow calculation of sherical silver nanoparticles concentration.
  5. Y. Cesbron, U. Shaheen, P. Free, R. Lévy; “TAT and HA2 Facilitate Cellular Uptake of Gold Nanoparticles but Do Not Lead to Cytosolic Localisation”, PLoS ONE 2015, 10(4): e0121683. doi: 10.1371/journal.pone.0121683.
  6. X. Chen, W. W. Qoutah, P. Free, J. Hobley, D. G. Fernig, D. Paramelle; “Features of Thiolated Ligands Promoting Resistance to Ligand Exchange in Self-Assembled Monolayers on Gold Nanoparticles”, Aust. J. Chem. 2012, 65, 266–274. doi: 10.1071/CH11432.

Other publications (reverse chronological):

  1. D. Paramelle, T. Peng, P. Free, D. G. Fernig, S. Lim, N. Tomczak; “Specific Internalisation of Gold Nanoparticles into Engineered Porous Protein Cages via Affinity Binding”, PLoS ONE 2016, 11(9): e0162848. doi: 10.1371/journal.pone.0162848.
  2. N. Zhang, X. Su, P. Free, X. Zhou, K. G. Neoh, J. Teng, W. Knoll; “Plasmonic Metal Nanostructure Array by Glancing Angle Deposition for Biosensing Application”, Sensors and Actuators B 2013, 183, 310–318. doi: 10.1016/j.snb.2013.03.088.
  3. Y. Cesbron, C. P. Shaw, J. P. Birchall, P. Free, and R. Lévy; “Stripy nanoparticles revisited.”, Small 2012, 8(24), 3714–3718. doi: 10.1002/smll.201001465.
  4. J. Hobley, D. Paramelle, P. Free, D. G. Fernig, S. Kajimoto, S. Gorelik, “Photothermal Laser Material Interactions — From the Sledgehammer to Nano-GPS”, in Advances in Bio-Imaging: From Physics to Signal Understanding Issues. State-of-the-Art and Challenges, Vol. 120/2012, Springer, 2012, 85–111.
  5. V. See, P. Free, Y. Cesbron, P. Nativo, U. Shaheen, D. Rigden, D. Spiller, D. Fernig, M. White, I. Prior, M. Brust, B. Lounis, R. Levy; “Cathepsin L Digestion of Nanobioconjugates upon Endocytosis”, ACS Nano 2009, 3, 2461–2468. doi: 10.1021/nn9006994.
  6. A. Ori, P. Free, J. Courty, M. C. Wilkinson, D. G. Fernig; “Identification of Heparin-binding Sites in Proteins by Selective Labeling”, Mol. Cell Proteomics 2009, 8, 2256–2265. doi: 10.1074/mcp.M900031-MCP200.
  7. N. Panchal, A. Fernandez-Yarza, P. Free, P. R. J. Gaffney; “Efficient preparation of 4-methoxy-5,6-dihydro-2H-pyran”, Tet. Lett. 2008, 49, 1836–38. doi: 10.1016/j.tetlet.2008.01.039.
  8. R. L. Charles, E. Schröder, G. May, P. Free, P. R. J. Gaffney, R. Wait, S. Begum, R. J. Heads, P. Eaton; “Protein Sulfenation as a Redox Sensor”, Mol. Cell Proteomics 2007, 6, 1473–84. doi: 10.1074/mcp.M700065-MCP200.
  9. P. Free, C. A. Hurley, T. Kageyama, B. M. Chain, A. B. Tabor; “Mannose–pepstatin conjugates as targeted inhibitors of antigen processing”, Org. Biomol. Chem. 2007, 4, 1817–30. doi: 10.1039/b600060f.
  10. B. M. Chain, P. Free, P. Medd, C. Swetman, A. B. Tabor, N. Terrazzini; “The Expression and Function of Cathepsin E in Dendritic Cells”, J. Immunol. 2005, 174, 1791–800. doi: 10.4049/jimmunol.174.4.1791.
  11. N. Kvirkvelia, I. Vojnovic, T. D. Warner, V. Athie-Morales, P. Free, N. Rayment, B. M. Chain, T. W. Rademacher, T. Lund, I. M. Roitt, P. J. Delves; “Placentally derived prostaglandin E2 acts via the EP4 receptor to inhibit IL-2-dependent proliferation of CTLL-2 T cells”, Clin. Exp. Immun. 2002, 127, 263–269. doi: 10.1046/j.1365–2249.2002.01718.x.
  12. K. Bryniarski, R. Biedroń, L. Petrovska, P. Free, B. M. Chain, J. Marcinkiewicz; “Phagocytosis of bacteria by mouse bone marrow-derived dendritic cells affects their ability to process a heterologous soluble antigen in vitro”, Cent-Europ. J. Immunol. 2000, 25(4), 210–215.