Publications

See also our Google Scholar page for a full publications and citations list

  1. M. M. Meirovich, O. Bachar, R. Nandi, N. Amdursky, and O. Yehezkeli, Tailoring QDs Sizes for Optimal Photoinduced Catalytic Activation of Nitrogenase, ChemSusChem 10.1002/cssc.202101676 (2021).
  2. A. Yucknovsky, B.B. Rich, A. Westfried, B. Pokroy, and N. Amdursky, Self-propulsion of droplets via light-stimuli rapid control of their surface tension, Adv. Mater. Interfaces 8, 2100751 (2021).
  3. A. Burnstine-Townley, S. Mondal, Y. Agam, R. Nandi, and N. Amdursky, Light-modulated cationic and anionic transport across protein biopolymers, Angew. Chem. Int. Ed. 60, 24676–24685 (2021).
  4. R. Nandi, Y. Agam, and N. Amdursky, A protein-based free-standing proton-conducting transparent elastomer for large-scale sensing applications, Adv. Mater. 23, 2101208 (2021).
  5. S. Mondal, N. Ghorai, S. Bhunia, H. N. Ghosh, and N. Amdursky, Long-range light-modulated charge transport across the molecular heterostructures doped protein biopolymers, Chem. Sci., 12, 8731-8739 (2021).
  6. Y. Agam, R. Nandi, T. Bulava and N. Amdursky, The role of the protein-water interface in dictating proton conduction across protein-based biopolymers, Mater. Adv. 2, 1739-1746 (2021).
  7. S. Das, P. Martin, G. Vasilyev, R. Nandi, N. Amdursky and E. Zussman, Processable, Ion Conducting Hydrogel for Flexible Electronic Devices with Self Healing Capability, Macromolecules, 53, 11130-11141 (2020).
  8. Y. Agam, R. Nandi, A. Kaushansky, U. Peskin and N. Amdursky, The porphyrin ring rather than the metal ion dictates long-range electron transport across proteins suggesting coherence-assisted mechanism, Proc. Natl. Acad. Sci. USA, 202008741 (2020).
  9. S. Mondal, Y. Agam and N. Amdursky, Enhanced proton conductivity across protein biopolymers mediated by doped carbon nanoparticles, Small. 16, 2005526 (2020). *Selected for a Cover image: Small 16, 2070272 (2020).
  10. I. Benisti, R. Nandi, N. Amdursky and Y. Paz, The photocatalytic behavior of various types of bismuth vanadate as studied by nanoseconds-resolved transient FTIR spectroscopy, Appl. Catal. B Environ. 278, 119351 (2020).
  11. R. Nandi, A. Yucknovsky, M.M. Mazo and N. Amdursky, Exploring the inner environment of protein hydrogels toward understanding their drug delivery capabilities J. Mater. Chem. B. 8, 6964-6974 (2020).
  12. N. Amdursky and Y. Lin, Tracking subtle membrane disruptions with a tethered photoacid, ChemPhotoChem 4, 592-600 (2020). *Selected for a Cover feature: ChemPhotoChem 4, 596 (2020).
  13. Y. Eshel, U. Peskin and N. Amdursky, Coherence-assisted electron diffusion across the multi-heme cytochrome based bacterial nanowire, Nanotechnology 31, 314002 (2020).
  14. S. Mondal, Y. Agam, R. Nandi and N. Amdursky, Exploring Long-range Proton Conduction, the Conduction Mechanism and Inner Hydration State of Protein Biopolymers, Chem. Sci. 11, 3547-3556 (2020).
  15. A. Burnstine-Townley, Y. Eshel and N. Amdursky, Conductive Scaffolds for Cardiac and Neuronal Tissue Engineering: Governing Factors and Mechanism. Adv. Funct. Mater. 30, 1901369 (2020).
  16. S. Mondal, A. Yucknovsky, K. Akulov, N. Ghorai, T. Schwartz, H.N. Ghosh and N. Amdursky, Efficient Photosensitizing Capabilities and Ultrafast Carrier Dynamics of Doped Carbon Dots, J. Am. Chem. Soc. 141, 15413-15422 (2019).
  17. A. Yucknovsky, S. Mondal, A. Burnstine-Townley, M. Foqara and N. Amdursky, Light controlled dynamic self-assembly of Au nanoparticles in aqueous and non-aqueous solutions by the use of photoacids and photobases, Nano Lett. 19, 3804-3810 (2019).
  18. N. Amdursky, Y. Lin, N. Aho and G. Groenhof, Exploring fast proton transfer events associated with lateral proton diffusion on the surface of membranes, Proc. Natl. Acad. Sci. USA 116, 2443-2451 (2019).
  19. N. Lapshina, I. Shishkin, R. Nandi, R. Noskov, H. Barhom, S. Joseph, T. Ellenbogen, A. Natan, P. Ginzburg, N. Amdursky and G. Rosenman, Bioinspired Amyloid Nanodots With Visible Fluorescence, Adv. Opt. Mater. 7, 1801400 (2019).
  20. N. Amdursky, E. Glowacki and P. Meredith, Macroscale Biomolecular Electronics and Ionics, Adv. Mater. 3, 1802221 (2019).
  21. N. Amdursky, M.M. Mazo, M.R. Thomas, E. Humphrey, J.L. Puetzer, J-P. St-Pierre, S. C. Skaalure, R.R. Richardson, C. Terracciano and M.M. Stevens, Elastic serum-albumin based hydrogels: mechanism of formation and application in cardiac tissue engineering, J. Mater. Chem. B 6, 5604-5612 (2018).
  22. C-C. Hsu, A. Serio, N. Amdursky, C. Besnard and M.M. Stevens, Fabrication of Hemin-Doped Serum Albumin-Based Fibrous Scaffolds for Neuronal Differentiation in Human iPSC-Derived Neural Stem Cells, ACS Appl. Mater. Interfaces 10, 5305-5317 (2018).
  23. S-T. Wang, Y. Lin, R.K. Spencer, M.R. Thomas, A.I. Nguyen, N. Amdursky, C. Song, P.A. Parmar, R.M. Morgan, P. Ercius, S. Aloni, R.N. Zuckermann and M.M. Stevens, Sequence-Dependent Self-Assembly and Structural Diversity of Islet Amyloid Polypeptide-Derived β-Sheet Fibrils, ACS Nano 11, 8579-8589 (2017).
  24. N. Amdursky, H. Rashid, M.M. Stevens and I. Yarovsly, Exploring proton diffusion across insulin amyloid fibril surfaces by naphthol-based photoacid fluorescence and molecular simulations, Sci. Rep. 7, 5247 (2017).
  25. N. Amdursky, X. Wang, P. Meredith, D.J. Riley, D.J. Payne, D.D.C. Bradley and M.M. Stevens, Electron Hopping Along Hemin-Doped Serum Albumin Mats on Centimetre-Length Scales, Adv. Mater. 29, 1700810 (2017).
  26. S-T. Wang, Y. Lin, C-C. Hsu, N. Amdursky, C.D. Spicer and M.M. Stevens, Probing Amylin Fibrillation at the Early Stage via a Tetracysteine-Targeting Fluorophore, Talanta 173, 44-50 (2017).
  27. S-T. Wang, Y. Lin, N. Todorova, Y. Xu, M. Mazo, S. Rana, V. Leonardo, N. Amdursky, I. Yarovsky, A. Edwards, S.J. Matthews, B.D. Alexander and M.M. Stevens, Facet Dependent Islet Amyloid Polypeptide Interactions with Gold Nanoparticles: Implications for Fibril Formation and Peptide-Induced Lipid Membrane Disruption, Chem. Mater. 29, 1550-1560 (2017).
  28. Y. Lin, E.T. Pashuck, M. Thomas, N. Amdursky, S.-T. Wang, L.W. Chow, M.M. Stevens, Plasmonic Chirality Imprinting on Nucleobase-Displaying Supramolecular Nanohelices by Metal–Nucleobase Recognition, Angew. Chem. Int. Ed. 56, 2361-2365 (2017).
  29. N. Amdursky, X. Wang, P. Meredith, D.D.C. Bradley and M.M. Stevens, Long-Range Proton Conduction Across Free-Standing Serum Albumin Mats, Adv. Mater. 28, 2692-2698 (2016).
  30. N. Amdursky, P.K. Kundu, J. Ahrens, D. Huppert and R. Klajn, Non-Covalent Interactions with Proteins Modify the Physicochemical Properties of Spiropyran, ChemPlusChem 81, 44-48 (2016).
  31. N. Amdursky, Photoacids as a new fluorescence tool for tracking structural transitions of proteins: Following the concentration-induced transition of bovine serum albumin, Phys. Chem. Chem. Phys. 17, 32023-32032 (2015).
  32. A.L.B. Maçon, S.J. Page, J.J. Chung, N. Amdursky, M.M. Stevens, J.V.M. Weaver, J.V. Hanna and J.R. Jones, A structural and physical study of sol-gel methacrylate-silica hybrids: Intermolecular spacing dictates the mechanical properties, Phys. Chem. Chem. Phys. 17, 29124-29133 (2015).
  33. N. Amdursky and M.M. Stevens, Circular Dichroism of Amino Acids: Insights into the Structural Formation of Phenylalanine, ChemPhysChem 16, 2768-2774 (2015).
  34. L. Santos, G. Fuhrmann, M. Juenet, N. Amdursky, C.M. Horejs, P. Campagnolo and M.M. Stevens, Extracellular stiffness modulates the expression of functional proteins and growth factors in endothelial cells, Adv. Healthcare Mater. 4, 2056-2063 (2015).
  35. N. Amdursky, Electron transfer across helical peptides, ChemPlusChem 80, 1075-1095 (2015).
  36. R. Simkovitch, K. Akulov, Y. Erez, N. Amdursky, R. Gepshtein, T. Schwartz and D. Huppert, Acid effect on excited Auramine-O molecular rotor relaxations in solution and adsorbed on insulin fibrils, Methods Appl. Fluoresc. 3, 034005 (2015).
  37. N. Amdursky, L. Sepunaru, S. Raichlin, I. Pecht, M. Sheves and D. Cahen, Electron Transfer Proteins as Electronic Conductors: Significance of the metal and its binding site in the blue Cu protein, Azurin, Adv. Sci. 2, 1400026 (2015).
  38. S. Semin, A. van Etteger, L. Cattaneo, N. Amdursky, L. Kulyuk, S. Lavrov, A. Sigov, E. Mishina , G. Rosenman and Th. Rasing, Strong Thermo-Induced Single And Two-Photon Green Luminescence In Self-Organized Peptide Microtubes, Small 11, 1156-1160 (2015).
  39. N. Amdursky, R. Simkovitch and D. Huppert, Excited-State Proton Transfer of Photoacids Adsorbed on Biomaterials, J. Phys. Chem. B 118, 13859-13869 (2014).
  40. N. Amdursky, D. Marchak, L. Sepunaru, I. Pecht, M. Sheves and D. Cahen, Electronic Transport via Proteins, Adv. Mater. 26, 7142-7161 (2014).
  41. N. Amdursky, D. Farber, C.A. Bortolotti, D.A. Dolgikh, R.V. Chertkova, I. Pecht, M. Sheves, and D. Cahen, Solid-State Electron Transport via Cytochrome C depends on Electronic Coupling to Electrodes and across the Protein, Proc. Natl. Acad. Sci. USA. 111, 5556-5561 (2014).
  42. Y. Bram, A. Frydman-Marom, I. Yanai, S. Gilead, R. Shaltiel-Karyo, N. Amdursky, and E. Gazit, Apoptosis induced by islet amyloid polypeptide soluble oligomers is neutralized by diabetes-associated specific antibodies, Sci. Rep. 4, 4267 (2014).
  43. N. Amdursky, G. Shalev, A. Handelman, S. Litsyn, A. Natan, Y. Roizin, Y. Rosenwaks, D. Szwarcman, and G. Rosenman, Bioorganic Diphenylalanine Nanodots: From Alzheimer Core Motif to Nonvolatile Memory, Appl. Phys. Lett. Mater. 1, 062104 (2013).
  44. N. Amdursky, D. Farber, I. Pecht, M. Sheves, and D. Cahen, Redox Activity Distinguishes Solid-State Electron Transport from Solution-Based Electron Transfer in a natural and artificial protein: Cytochrome C and Hemin-Doped Human Serum Albumin, Phys. Chem. Chem. Phys. 15, 17142-17149 (2013).
  45. N. Amdursky, Enhanced solid-state electron transport via tryptophan containing peptide networks, Phys. Chem. Chem. Phys. 15, 13479-13482 (2013).
  46. N. Amdursky, I. Pecht, M. Sheves, and D. Cahen, Electron Transport via Cytochrome C on Si-H Surfaces: Roles of Fe and Heme, J. Am. Chem. Soc. 135, 6300-6306 (2013).
  47. I. Presiado, S. Shomer, Y. Erez, R. Gepshtein, N. Amdursky, and D. Huppert, Time-Resolved Emission of Retinoic Acid, J. Photochem. Photobiol. A 258, 30-40 (2013).
  48. N. Amdursky, I. Pecht, D. Cahen, and M. Sheves, Marked changes in electron transport through the blue copper protein azurin in the solid state upon deuteration, Proc. Natl. Acad. Sci. USA. 110, 507-512 (2013).
  49. N. Amdursky, I. Pecht, M. Sheves, and D. Cahen, Doping Human Serum Albumin with Retinoate Markedly Enhances Electron Transport Across the Protein, J. Am. Chem. Soc. 134, 18221–18224 (2012).
  50. W. Li, L. Sepunaru, N. Amdursky, I. Pecht, M. Sheves, and D. Cahen, Temperature and Force Dependence of Nanoscale Electron Transport via the Cu Protein Azurin, ACS Nano 6, 10816-10824 (2012).
  51. Y. Erez, N. Amdursky, R. Gepshtein, and D. Huppert, Temperature and Viscosity Dependence of the Nonradiative Decay Rates of Auramine-O and Thioflavin-T in Glass-Forming Solvents, J. Phys. Chem. A 116, 12056-12064 (2012).
  52. N. Amdursky, and D. Huppert, Auramin-O as a Fluorescence Marker for the Detection of Amyloid Fibrils, J. Phys. Chem. B 116, 13389-13395 (2012).
  53. N. Amdursky, Y. Erez, and D. Huppert, Molecular Rotors: What Lies Behind the High Sensitivity of the Thioflavin-T Fluorescent Marker, Acc. Chem. Res. 45, 1548-1557 (2012).
  54. N. Amdursky, E. Gazit, and G. Rosenman., Formation of low-dimensional crystalline nucleus region during insulin amyloidogenesis process, Biochem. Biophys. Res. Commun. 419, 232-237 (2012).
  55. N. Amdursky, A. Handelman, and G. Rosenman, Optical transition induced by molecular transformation in peptide nanostructures, Appl. Phys. Lett. 100, 103701 (2012). *Selected for the Virtual Journal of Nanoscale Science & Technology, 25(12) (2012).
  56. A. Handelman, P. Beker, N. Amdursky, and G. Rosenman, Physics and Engineering of Peptide Supramolecular Nanostructures, Phys. Chem. Chem. Phys. 14, 6391-6408 (2012).
  57. A. Handelman, P. Beker, E.D. Mishina, S. Semin, N. Amdursky, and G. Rosenman, Ferroelectric Properties and Phase Transition in Dipeptide Nanotubes, Ferroelectrics 430, 84-91 (2012).
  58. A.V. Kudryavtsev, K.V. Shvyrkov, E.D. Mishina, A. S. Sigov, A. Handelman, N. Amdursky, and G. Rosenman, Bioferroelectricity and Biopiezelectricity, Phys. Solid State 54, 1263-1268 (2012).
  59. N. Amdursky, P. Beker, I. Koren, B. Bank-Srour, E. Mishina, S. Semin, T. Rasing, Y. Rosenberg, Z. Barkay, E. Gazit, and G. Rosenman, Structural Transition in Peptide Nanotubes, Biomacromolecules 12, 1349-1354 (2011).
  60. N. Amdursky, R. Gepshtein, Y. Erez, and D. Huppert, Pressure effect on the nonradiative process of thioflavin-T, J. Phys. Chem. A 115, 6481-6487 (2011).
  61. T. Hutter, N. Amdursky, R. Gepshtein, S.R. Elliott and D. Huppert, Study of Thioflavin-T Immobilized in Porous Silicon and the Effect of Different Organic Vapours on the Fluorescence Lifetime, Langmuir 27, 7587-7594 (2011).
  62. Y. Erez, Y.H. Liu, N. Amdursky and D. Huppert, Modeling the nonradiative decay rate of electronically-excited ThT, J. Phys. Chem. A 115, 8479-8487 (2011).
  63. N. Amdursky, I. Koren, E. Gazit, and G. Rosenman., Adjustable Photoluminescence of Peptide Nanotubes Coatings, J. Nanosci. Nanotechnol. 11, 9282-9286 (2011).
  64. N. Amdursky, R. Gepshtein, Y. Erez, and D. Huppert, Temperature Dependence of the Fluorescence Properties of Thioflavin-T in Propanol, a Glass-Forming Liquid, J. Phys. Chem. A 115, 2540-2548 (2011).
  65. N. Amdursky, M. Molotskii, E. Gazit, and G. Rosenman., Elementary building blocks of self-assembled peptide nanotubes, J. Am. Chem. Soc. 132, 15632–15636 (2010).               *Discussed Also: Nature News & Views section: Nature, 468, 516-517 (2010).
  66. P. Beker, I. Koren, N. Amdursky, E. Gazit, and G. Rosenman, Bioinspired Peptide Nanotubes as Supercapacitor Electrodes, J. Mater. Sci. 45, 6374-6378 (2010).
  67. N. Amdursky, P. Beker, J. Schklovsky, E. Gazit, and G. Rosenman, Ferroelectric and Related Phenomena in Biological and Bioinspired Nanostructures, Ferroelectrics 399, 107-117 (2010).
  68. N. Amdursky, E. Gazit, and G. Rosenman, Quantum Confinement in Self-Assembled Bio-Inspired Peptide Hydrogels, Adv. Mater. 22, 2311-2315 (2010).
  69. J. Shklovsky, P. Beker, N. Amdursky, E. Gazit and G. Rosenman, Bioinspired Peptide Nanotubes: Deposition Technology and Physical Properties, Mater. Sci. Eng. B. 169, 62-66 (2010).
  70. A. Kholkin, N. Amdursky, I. Bdikin, E. Gazit, and G. Rosenman, Strong Piezoelectricity in bioinspired nanotubes, ACS Nano 4, 610-614 (2010).
  71. I. Torchinsky, N. Amdursky, A.Inberg and G. Rosenman, Electron-Induced Adhesion and Patterning of Gold Nanoparticles, Appl. Phys. Lett. 96, 093106 (2010).
  72. N. Amdursky, R. Orbach, E. Gazit and D. Huppert, Probing the inner cavities of hydrogels by proton diffusion, J. Phys. Chem. C 113, 19500-19505 (2009).
  73. N. Amdursky, M. Molotskii, D. Aronov, L. Adler-Abramovich, E. Gazit, and G. Rosenman, Blue luminescence based on quantum confinement at peptide nanotubes, Nano Lett. 9, 3111-3115 (2009).
  74. N. Amdursky, M. Molotskii, E. Gazit, and G. Rosenman, Self-assembled Bio-Inspired Quantum Dots: Optical Properties, Appl. Phys. Lett. 94, 261907 (2009).
  75. R. Gepshtein, D. Huppert, I. Lubitz, N. Amdursky and A.B. Kotlyar, Radiationless transition of G4 wires and dGMP, J. Phys. Chem. C 112, 12249-12258 (2008).