Poul Martin Bendix, Ph.D, Associate Professor

My family name was "Hansen" until 06/2007

Address: Blegdamsvej 17, Niels Bohr Institute, University of Copenhagen
phone: 35325251

Research Interests


  • (2015-2019) Sapere Aude grant (Danish Council for Independent Research)
  • (2014-2016) Editorial board of Scientific Reports
  • (2012) Associated Professor at the Niels Bohr Institute
  • (2011) Assistant Professor at the Niels Bohr Institute
  • (2009-2010) Postdoc in "Boxer Lab" at Stanford University.
  • (2009) Postdoc at the Niels Bohr Institute at The University of Copenhagen.
  • (2007-2009) Postdoc at the Nanoscience Center at The University of Copenhagen.
  • (2007) Ph.D-degree in Biophysics at Niels Bohr Institute, University of Copenhagen.
  • (2006) Graduate student at Harvard University.
  • (2003) Cand. Scient. of physics at the University of Copenhagen.
  • (2001) Bachelor of physics and mathematics at the University of Copenhagen.

    Major Grants/Awards

  • (2015-2019) Sapere Aude starting grant (Danish Council for Basic Research)
  • (2015-2018) Novo Synergy Programme (Co-applicant).
  • (2012-2015) Young Investigator Award (Villum Foundation)
  • (2011) Postdoc grant (Carlsberg Foundation)
  • (2010) Postdoc grant (Danish Council for Basic Research)
  • Person


    Membrane dynamics
    Current topics include membrane-protein interactions with regard to membrane deformation or curvature sensing by BAR domains. Also, we study the dynamics of membrane tubes of both cells and simple model membrane tubes. Finally, we study membrane phase behavior which has important implications for the lateral organization of membranes as wells as for physical properties like bending, permeability and elasticity.

    Membrane fusion
    At Stanford University, Boxer lab, I worked on membrane fusion of small unilamellar lipid vesicles to flat membranes tethered to glass surfaces. This geometry closely resembles biological systems in which liposomes fuse to plasma membranes. The fusion mechanism was studied using DNA zippering between complementary strands linked to the two apposing membranes closely mimicking the zippering mechanism of SNARE fusion complexes.

    Cytoskeletal dynamics
    At Harvard University, Harvard soft matter group, I worked with reconstitutted contractile acto-myosin systems containing mainly actin, actin cross-linkers and myosin motors. Contractility and rheology of such systems was studied using confocal microscopy and rheology.

    Effect of membrane curvature on lateral distribution of membrane proteins
    Several membrane proteins exhibit interesting shapes that increases their preference for certain membrane curvatures. Both peripheral and transmembrane proteins are tested with respect to their affinity for a spectrum of high membrane curvatures. We generate high membrane curvatures by pulling membrane tubes out of Giant Unilamellar lipid Vesicles (GUVs). The tube diameter can be tuned by aspirating the GUV into a micropipette for controlling the membrane tension. By using fluorescently labled proteins we have shown that sorting of proteins like e.g. FBAR onto tubes is significantly increased for highly curved tubes (small tube diameter).

    Membrane adhesion and phase behavior
    At the Nanoscience center KU I worked with adhesion of membranes to substrates using advances quantitative microscopy techniques. Also, I studied phase behavior of small unilamellar lipid vesicles with respect to their curvature.

    Optical properties of nanoparticles
    At the NBI I am involved in projects relating to optical properties of metallic nanoparticles in particular with respect to plasmonic heating with direct applications to photothermal cancer therapy. For this purpose we have developed heating assays that can be used to measure the heating of any nanoscopic heat source like an irradiated nanoparticle.

    "The most beautiful thing we can experience is the mysterious. It is the source of all true art and science. He to whom this emotion is a stranger, who can no longer pause to wonder and stand rapt in awe, is as good as dead: his eyes are closed."
    Albert Einstein

    Last updated Aug 2016