• Nadine Döge, Sabrina Hadam, Pierre Volz, Karl-Heinz Schönborn, Ulrike Blume-Peytavi, Ulrike Alexiev and Annika Vogt
    Identification of polystyrene nanoparticle penetration across intact skin barrier as rare event at sites of focal particle aggregations
    Journal of Biophotonics , 2018 doi: 10.1002/jbio.201700169

  • Pierre Volz, Robert Brodwolf, Christian Zoschke, Rainer Haag, Monika Schäfer-Korting and Ulrike Alexiev
    White-Light Supercontinuum Laser-Based Multiple Wavelength Excitation for TCSPC-FLIM of Cutaneous Nanocarrier Uptake
    Z. Phys. Chem. , 2018 doi: 10.1515/zpch-2017-1050


  • P Volz, P Schilrreff, R Brodwolf, C Wolff, J Stellmacher, J Balke, M Morilla, C Zoschke, M Schäfer-Korting, U Alexiev
    Pitfalls in using fluorescence tagging of nanomaterials:tecto-dendrimers in skin tissue as investigated by Cluster-FLIM
    Ann. N.Y. Acad. Sci., 1405, 202-214, 2017. DOI: 10.1111/nyas.13473

  • M Radbruch, H Pischon, A Ostrowski, P Volz, R Brodwolf, F Neumann, M Unbehauen, B Kleuser, R Haag, N Ma, U Alexiev, L Mundhenk, A Gruber.
    Dendritic Core-Multishell Nanocarriers in Murine Models of Healthy and Atopic Skin.
    Nanoscale Res Lett 12(64), 2017. doi: 10.1186/s11671-017-1835-0

  • U Alexiev,  P Volz, A Boreham, R Brodwolf.
    Time-resolved fluorescence microscopy (FLIM) as an analytical tool in skin nanomedicine.
    Eur J Pharm Biopharm. 2017. doi: 10.1016/j.ejpb.2017.01.005

  • L Lowenau, C Zoschke ,R Brodwolf, P Volz, C Hausmann, S Wattanapitayakul, A Boreham, U Alexiev, M Schafer-Korting.
    Increased permeability of reconstructed human epidermis from UVB-irradiated keratinocytes.
    Eur J Pharm Biopharm. 2017. doi: 10.1016/j.ejpb.2016.12.017

  • A Boreham, R Brodwolf, K Walker, R Haag, U Alexiev.
    Time-Resolved Fluorescence Spectroscopy and Fluorescence Lifetime Imaging Microscopy for Characterization of Dendritic Polymer.
    Molecules 22 (1), 17, 2017, doi:10.3390/molecules22010017

  • F Escobar, C Lang, A Takiden, C Schneider, J Balke, J Hughes, U Alexiev, P Hildebrandt , M Mroginski.
    Protonation-Dependent Structural Heterogeneity in the Chromophore Binding Site of Cyanobacterial Phytochrome Cph1.
    J. Phys. Chem. B, 2017, 121 (1), 47–57 DOI: 10.1021/acs.jpcb.6b09600

  • A Boreham, P Volz, D Peters, C. Keck, U Alexiev.
    Determination of nanostructures and drug distribution in lipid nanoparticles by single molecule microscopy.
    Eur J Pharm Biopharm 110, 31-38, 2017. doi: 10.1016/j.ejpb.2016.10.020

  • H Pischon, M Radbruch, A Ostrowski, P Volz, C Gerecke, M Unbehauen, S Hönzke, S Hedtrich, J Fluhr, R Haag, B Kleuser, U Alexiev, A Gruber, L Mundhenk.
    Stratum corneum targeting by dendritic core-multishell-nanocarriers in a mouse model of psoriasis.
    Nanomedicine 13(1), 317-327, 2017. DOI: 10.1016/j.nano.2016.09.004



  • G Zoubari, S Staufenbiel, P Volz, U Alexiev, R Bodmeier.
    Effect of drug solubility and lipid carrier on drug release from lipid nanoparticles for dermal delivery.
    Eur J Pharm Biopharm
    110: 39–46. 2016.

  • N Zhang, A Said, C Wischke, V Kral, R Brodwolf, P Volz, A Boreham, C Gerecke, W Li, A Neffe, B Kleuser, U Alexiev, A Lendlein, M Schäfer-Korting.
    Poly[acrylonitrile-co-(N-vinyl pyrrolidone)] nanoparticles -composition-dependent skin penetration enhancement of a dye probe andbiocompatibility.
    Eur J Pharm Biopharm. 2016. doi: 10.1016/j.ejpb.2016.10.019

  • A Vogt,C Wischke, AT Neffe, N Ma, RH Müller, U Alexiev, A Lendlein.
    Nanocarriers for drug delivery into and through the skin: Do existing technologies match clinical challenges?
    J. Contr. Release. 242, 3-15, 2016. doi: 10.1016/j.jconrel.2016.07.027

  • P Volz, N Krause, J Balke, C Schneider, M Walter, F Schneider, R Schlesinger, U Alexiev.
    Light and pH-induced changes in structure and accessibility of transmembrane helix B and its immediate environment in Channelrhodopsin-2.
    J. Biol. Chem. 291, 33, 17382-17393, 2016. doi: 10.1074/jbc.M115.711200

  • A Wolf, C Schneider, TY Kim, K Kirchberg, P Volz, U Alexiev.
    A simulation-guided fluorescence correlation spectroscopy tool to investigate to protonation dynamics of cytrochrome c oxidase.
    Phys. Chem. Chem. Phys.18, 12877-12885, 2016. doi: 10.1039/c5cp07925j.

  • RH Müller, U Alexiev, P Sinambela, CM Keck.
    Nanostructured Lipid Carriers (NLC): The Second Generation of Solid Lipid Nanoparticles. In: Percutaneous Penetration Enhancer Chemical Methods in Penetration Enhancement: Nanocarriers, Eds. Nina Dragicevic, Howard I. Maibach (Springer). 2016

  • A Boreham, J Pikkemaat, P Volz, R Brodwolf, C Kuehne, K Licha, R Haag, J Dernedde, U Alexiev.
    Detecting and Quantifiying Biomolecular Interactions of a Dendritic Polyglycerol Sulfate Nanoparticle Using Fluorescence Lifetime Measurements.
    21(1), 22. 2016. doi:10.3390/molecules21010022


  • C Richter, C Schneider, MT Quick, P Volz, R Mahrwald, J Hughes, B Dick, U Alexiev, NP Ernsting.
    Dual-fluorescence pH probe for bio-labelling.
    Phys. Chem. Chem. Phys. 2015. doi: 10.1039/c5cp05454k

  • M Witting, A Boreham, R Brodwolf, K Vavrova, U Alexiev, W Friess, S. Hedtrich.
    Interactions of Hyaluronic Acid with the Skin and Implications for the Dermal Delivery of Biomacromolecules.
    Molecular Pharmaceutics. 2015. doi: 10.1021/mp500676e

  • P Volz, A Boreham, A. Wolf, TY Kim, J Balke, J Frombach, S Hadam, Z Afraz, F Rancan, U Blume-Peytavi, A Vogt, U Alexiev.
    Application of Single Molecule Fluorescence Microscopy to Characterize the Penetration of a Large Amphiphilic Molecule in the Stratum Conerum of Human Skin.
    International Journal of Molecular Sciences
    . 16(4), 6960-69772015. doi:10.3390/ijms16046960

  • A Ostrowski, D Nordmeyer, A Boreham, C Holzhausen, L Mundhenk, C Graf, MC Meinke, A Vogt, S Hadam, J Lademann, E Rühl, U Alexiev, AD Gruber.
    Overview on the Localization of Nanoparticles in Tissue and Cellular Context by Different Imaging Techniques.
    Beilstein Journal of Nanotechnology 6: 263-80. 2015. doi:10.3762/bjnano.6.25

  • YJ Zhu, CS Choe, S Ahlberg, MC Meinke, U Alexiev, J Lademann, ME Darvin.
    Penetration of silver nanoparticles into porcine skin ex vivo using fluorescence lifetime imaging microscopy, Raman microscopy and surface enhanced Raman scattering microscopy.
    J. Biomed. Opt. 2015. doi:10.1117/1.JBO.20.5.051006

  • J Lademann, F Knorr, H Richter, S Jung, MC Meinke, E Rühl, U Alexiev, M Calderon, A Patzelt.
    Hair follicles as a target structure for nanoparticles.
    Journal of Innovative Optical Health Sciences
    . 2015. doi: 10/1142/S1793545815300049


  • A Boreham, R Brodwolf, M Pfaff, T-Y Kim, T Schlieter, L Mundhenk, AD Gruber, D Gröger, K Licha, R Haag, and U Alexiev. Temperature and environment dependent dynamic properties of a dendritic polyglycerol sulfate.
    Polym. Adv. Technol. 2014. doi: 10.1002/pat.3355

  • U Alexiev, DL Farrens.
    Fluorescence spectroscopy of rhodopsins: Insights and approaches.
    Biochim Biophys Acta.
    2014 May. 1837(5), SI: 694-709.

    A Ostrowski, D Nordmeyer, A Boreham, R Brodwolf, L Mundhenk, JW Fluhr, J Lademann, C Graf, E Rühl, U Alexiev, AD Gruber. Skin barrier disruptions in tape stripped and allergic dermatitis models have no effect on dermal penetration and systemic distribution of AHAPS-functionalized silica nanoparticles.
    . 2014 Apr 22. pii: S1549-9634(14)00187-7. doi: 10.1016/j.nano.2014.04.004.

  • N Alnasif, C Zoschke, E Fleige, R Brodwolf, A Boreham, E Rühl, KM Eckl, HF Merk, HC Hennies, U Alexiev, R Haag, S Küchler, M Schäfer-Korting. Penetration of normal, damaged and diseased skin - An in vitro study on dendritic core-multishell nanotransporters.
    J Control Release. 2014 Jul 10;185:45-50. doi: 10.1016/j.jconrel.2014.04.006. Epub 2014 Apr 13.

  • A Boreham, M Pfaff, E Fleige, R Haag, U Alexiev., Nanodynamics of dendritic core-multishell nanocarriers.
    . 2014 Feb 18;30(6):1686-95. doi: 10.1021/la4043155. Epub 2014 Feb 5.


  • C Hoppmann, U Alexiev, E Irran, K Rück-Braun.
    Synthesis and fluorescence of xanthone amino acids,
    Tetrahedron Letters
    , 2013 Aug 21, 54, 34, 4585-4587

  • K Kirchberg, H Michel, U Alexiev. 
    Exploring the entrance of proton pathways in cytochrome c oxidase from Paracoccus denitrificans: surface charge, buffer capacity and redox-dependent polarity changes at the internal surface.
    Biochim Biophys Acta.
    2013 Mar;1827(3):276-84

  • U Alexiev.
    Dynamics of Helix 8 in GPCR Function.
    Encyclopedia of Biophysics
    , 978-3-642-16711-9, 2013, pp 549-552

  • CM Keck, A Boreham, T Schlieter, D Peters, RH Müller, U Alexiev.
    Nanostructures and drug distribution within Nanostructured Lipid Carriers (NLC), In: “Proceedings of the 40th Annual Meeting of the Controlled Release Society (CRS)” ID 100536 (2013).




  • K. Kirchberg, H. Michel, and U. Alexiev.
    Net Proton Uptake Is Preceded by Multiple Proton Transfer Steps upon Electron Injection into Cytochrome c Oxidase. J. Biol. Chem., 2012, 287, 8187-93


  • T.-Y. Kim , T. Schlieter , S. Haase, and U. Alexiev.
    Activation and molecular recognition of the GPCR rhodopsin - Insights from time-resolved fluorescence depolarisation and single molecule experiments.
    Eur J Cell Biol.
    , 2012, 91, 300-310



  • A. Boreham, T.-Y. Kim, V. Spahn, C. Stein, L. Mundhenk, A. D. Gruber, R. Haag, P. Welker, K. Licha, and U. Alexiev.
    Exploiting fluorescence lifetime plasticity in FLIM: Target molecule localisation in cells and tissues.
    ACS Med. Chem. Lett., 2011, 2 (10), 724–728


  • K. Kirchberg, T.-Y. Kim, M. Möller, D. Skegro, G. Dasara Raju, J. Granzin, G. Büldt, R. Schlesinger, and U. Alexiev.
    Conformational dynamics of helix-8 in the GPCR rhodopsin controls arrestin activation in the desensitization process. 
    , 2011, 108 (46), 18690-18695



  • A. Dutta, K. C. Tirupula, U. Alexiev, and J. Klein-Seetharaman.
    Characterization of membrane protein non-native states. 1. Extent of unfolding and aggregation of rhodopsin in the presence of chemical denaturants.
    , 2010, 49, 6317-6328

  • A. Dutta, T.-Y. Kim, M. Moeller, J. Wu, U. Alexiev, and J. Klein-Seetharaman.
    Characterization of membrane protein non-native states. 2. The SDS-unfolded states of rhodopsin.
    , 2010, 49, 6329-6340

  • K. Kirchberg, T.-Y. Kim, S. Haase, and U. Alexiev.
    Functional interaction structures of the photochromic retinal protein rhodopsin. Photochem.
    Photobiol. Sci.
    , 2010, 9, 226-33





  • D. Narzi, K. Winkler, J. Saidowsky, R. Misselwitz, A. Ziegler, R.A. Böckmann, and U. Alexiev
    Molecular determinants of MHC class I complex stability: Shaping antigenic features through long-range electrostatic interactions.
    J. Biol. Chem. 2008, 283, 23093-23103



  • K. Winkler, A. Winter, C. Rückert, B. Uchanska-Ziegler, and U. Alexiev.
    Natural MHC Class I Polymorphism Controls the Pathway of Peptide Dissociation from HLA-B27 complexes.
    Biophys. J., 2007, 93(8),  2743-55

  • K. Winkler, J. Saidowsky, A. Ziegler, and U. Alexiev.
    Molecular determinants of MHC class I stability.
    In:International Proceedings of the 13th International Congress of Immunology (Kalil, J. et al eds.), Medimont Bologna (2007) ISBN 978-88-7587-379-0

  • T.-Y. Kim, K. Winkler, and U. Alexiev.
    Picosecond Multi-dimensional Fluorescence Spectroscopy: A tool to measure real-time protein dynamics during function.
    Photochemistry and Photobiology 83, 378-384 (2007)

  • N. Lehmann, U. Alexiev, and K. Fahmy.
    Linkage Between the Intramembrane H-bond Network Around Aspartic Acid83 and the Cytosolic Environment of Helix 8 in Photoactivated Rhodopsin.
    J. Mol. Biol. 366, 1129-1141 (2007)



  • B. Uchanska-Ziegler, U. Alexiev, R. Hillig, M. Hülsmeyer, T. Pöhlmann, W. Saenger, A. Volz, and A. Ziegler.
    X-ray crystallography and dynamic studies of HLA-B*2705 and B*2709 molecules complexed with the same peptide.
    In: Immunobiology of the Human MHC: Proceedings of the 13th International Histocompatibility Workshop and Conference (Hansen, J.A., ed.), IHWG Press, Seattle (2006) ISBN:0-945278-03-9


  • G. Schröder, U. Alexiev, and H. Grubmüller.
    Simulation of fluorescence anisotropy experiments: Probing protein dynamics.
    Biophys. J. 89(6), 3757-70 (2005)

  • A. Selle, C. Kappelt, M. A. Bader, G. Marowsky, K. Winkler, U. and Alexiev.
    Picosecond pulse induced two-photon fluorescence enhancement in biological material applying grating waveguide structures.
    Optics Lett. 30, 1683-1685 (2005)

  • V. Jaakola, M. Rehn, M. Möller, U. Alexiev, A. Goldman, and G. J. Turner.
    G-protein-coupled receptor domain over-expression in Halobacterium salinarium: Long-range allosteric interactions from the intracellular to the extracellular side in heptahelical membrane proteins.
    Proteins 60, 412-23 (2005)

  • M. Hülsmeyer, K. Welfle, T. Pöhlmann, R. Misselwitz, U. Alexiev, H. Welfle, W. Saenger, B. Uchanska- Ziegler, and A. Ziegler.
    Thermodynamic and structural equivalence of two HLA-B27 subtypes complexed with a Self-peptide.
    J. Mol. Biol. 346, 1367-1379 (2005)



  • T. Pöhlmann, R. A. Böckmann, H. Grubmüller, B. Uchanska-Ziegler, A. Ziegler, and U. Alexiev.
    Differential peptide dynamics is linked to MHC polymorphism.
    J. Biol. Chem. 279, 28197-28201 (2004)



  • U. Alexiev, I. Rimke, and T. Pöhlmann.
    Elucidation of the nature of the conformational changes of the EF-interhelical loop in  bacteriorhodopsin and of the helix VIII on the cytoplasmic surface of rhodopsin: A time-resolved fluorescence depolarization study.
    J. Mol. Biol. 328, 705-719 (2003)

  • B. Uchanska-Ziegler, U. Alexiev, R. Hillig, M. Hülsmeyer, T. Pöhlmann, W. Saenger, A. Volz, and A. Ziegler (2003).
    In HLA 2002. The immunobiology of the human MHC. Eds. Dupont B, Hansen J. IHWG Press, Seattle



  • T. Mielke, U. Alexiev, M. Gläsel, H. Otto, and M. P. Heyn.
    Light-induced changes in the structure and accessibility of the cytoplasmic loops of rhodopsin in the activated MII-state.
    Biochemistry 41, 7875-84 (2002)

  • R. A. Krebs, U. Alexiev, R. Parthasarathy, A.-M. DeVita, and  M. S. Braiman.
    Detection of light-activated H+-release and M-intermediate formation from purified proteorhodopsin.
    BMC Physiology 2 (2002)



  • U. Alexiev, R. Mollaaghababa, H. G. Khorana, and M. P. Heyn.
    Evidence for long range allosteric interactions between the extracellular  and cytoplasmic parts of bacteriorhodopsin from the mutant R82A and its second site revertant R82A/G231C.
    J. Biol. Chem. 275, 13431-13440 (2000)

  • K. Heyne, J. Herbst, B. Dominguez  Herradon, U. Alexiev, and R. Diller.
    Reaction control in bacteriorhodopsin: Impact of Arg82 and Asp85 on the fast retinal isomerization, studied in the second site revertant Arg82Ala/Gly231Cys and various purple and blue forms of bacteriorhodopsin.
    Phys. Chem. B 104, 6053-6058 (2000)

  • M. S. Hutson, U. Alexiev , S. V. Shilov, K. J. Wise, and M. S. Braiman.
    Evidence for a perturbation of Arginine-82 in the bacteriorhodopsin photocycle from Time-­resolved Infrared spectra.
    Biochemistry 39, 13189-13200 (2000)



  • W. Behrens, U. Alexiev, R. Mollaaghababa, H. G. Khorana, and M. P. Heyn
    Structure of the interhelical loops and carboxyl terminus of bacteriorhodopsin by X-ray diffraction using site-directed heavy-atom labeling.
    Biochemistry 37, 10411-10419 (1998)

  • K. Heyne, R. Dziewior, R. Diller, and U. Alexiev.
    Single and double mutants of bacteriorhodopsin and their impact on photoisomerization.
    In Springer Series in Chemical Physics: "Ultrafast phenomena XI". Eds. T. Elsaesser, J.G. Fujimoto, D. A. Wiersma, W. Zinth, 681-683 (1998)



  • S. Moltke, U. Alexiev, and M. P. Heyn.
    Kinetics of light-induced intramolecular charge transfer and proton release in bacteriorhodopsin.
    Israel. J. Chem. 35, 235-248 (1996)



  • U. Alexiev, R. Mollaaghababa, P. Scherrer, H. G. Khorana, and M. P. Heyn.
    Rapid long ­range proton diffusion along the surface of the purple membrane and delayed proton transfer into the bulk.
    PNAS 92, 372-376 (1995)

  • U. Alexiev, P. Scherrer,  T. Marti,  H. G. Khorana, and M. P. Heyn.
    Time-resolved surface charge change on the cytoplasmic side of bacteriorhodopsin.
    FEBS Letters 373, 81-84 (1995)

  • S. Dickopf, U. Alexiev, M. P. Krebs, H. Otto, R. Mollaaghababa, H. G. Khorana, and M. P. Heyn.
    Proton transport by a bacteriorhodopsin mutant, aspartic acid-85—> asparagine, initiated in the unprotonated Schiff base state.
    PNAS 92, 11519-11523 (1995)



  • U. Alexiev, T. Marti, M. P. Heyn, H. G. Khorana, and P. Scherrer.
    Surface charge of bacteriorhodopsin detected with covalently bound pH-indicators at selected extracellular and cytoplasmic sites.
    Biochemistry 33, 298 - 306 (1994)

  • P. Scherrer, U. Alexiev, T. Marti, H. G. Khorana, and M. P. Heyn.
    Covalently bound pH­indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. I. Light­induced proton release kinetics and proton migration along the surface of bacteriorhodopsin micelles.
    Biochemistry 33, 13684-13699 (1994)

  • U. Alexiev, T. Marti, M. P. Heyn, H. G. Khorana, and  P. Scherrer.
    Covalently bound pH­indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin.  II. Rotational orientation of helices D and E and kinetic correlation between M-formation and proton release in bacteriorhodopsin micelles.
    Biochemistry 33, 13693-13699 (1994)



  • P. Scherrer, U. Alexiev, M. P. Heyn, T. Marti, and H.G. Khorana.
    Proton movement and surface charge in bacteriorhodopsin detected by selectively attached pH-indicators.
    In Structures and Functions of Retinal Proteins. Ed. J.L. Rigaud. Colloque INSERM/John Libbey Eurotext Ltd. Vol. 221: 205 - 211 (1992)

  • D. A. Greenhalgh, S. Subramaniam, U. Alexiev, H. Otto, M. P. Heyn, and H. G.  Khorana.
    Effect of introducing different carboxylate-containing side chains at position 85 on chromophore formation and proton transport in bacteriorhodopsin.
    J. Biol. Chem. 267, 25734-25738 (1992)