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Structure of Actin Cross-Linked with α-Actinin: A Network of Bundles

Physical Review Letters 2003年第14期91卷 148102-148102页

作者： O. Pelletier E. Pokidysheva L. S. Hirst N. Bouxsein Y. Li C. R. Safinya Materials Department Physics Department Biomolecular Science and Engineering Program University of California

Three-dimensional laser scanning confocal microscopy has revealed that filamentous actin, when complexed with the cross-linking protein α-actinin, will spontaneously assemble on a micron scale into a structure comprised of a relatively rigid, frequently branching, 3D network of bundles with characteristic mesh size of the order of the persistence length of F-actin. In contrast, additional nanoscale ordering is observed, as synchrotron x-ray diffraction has revealed a disordered, distorted square lattice of actin fibers within the individual bundles.

关键词： .branching laments cytoskeleton square lattice bundling mesh size actin rods micron scale Network of Bundles Actinin

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Lamellar Phase of Stacked Two-Dimensional Rafts of Actin Filaments

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Physical Review Letters 2003年第1期91卷 018103-018103页

作者： Gerard C. L. Wong Alison Lin Jay X. Tang Youli Li Paul A. Janmey Cyrus R. Safinya Materials Department Physics Department Biomolecular Science and Engineering Program University of California Santa Barbara California 93106 USA Physics Department Brown University Providence Rhode Island 02912 USA Institute for Medicine and Engineering University of Pennsylvania Philadelphia Pennsylvania 19104 USA

We examined liquid crystalline phases of the cytoskeletal polyelectrolyte filamentous (F-)actin in the presence of multivalent counterions. As a function of increasing ion concentration, the F-actin rods in either an isotropic or a nematic phase will transform into a new and unexpected lamellar phase of cross-linked rafts (LXR phase), before condensing into a bundled phase of parallel, close-packed rods. This behavior is generic for alkali earth divalent ions Mg2+, Ca2+, Sr2+, and Ba2+, and the structural transitions are achieved without any architecture-specific actin-binding linker proteins.

关键词： .lamellar liquid crystalline VOLUME NUMBER week ion concentration counterions rafts divalent multivalent actin rods LXR bundled phase

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Structural polymorphism of DNA-dendrimer complexes

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Physical Review Letters 2003年第7期91卷 075501-075501页

作者： Heather M. Evans A. Ahmad K. Ewert T. Pfohl A. Martin-Herranz R. F. Bruinsma C. R. Safinya Materials Department Physics Department and Biomolecular Science and Engineering Program University of California Santa Barbara California 93106 USA Department of Physics and Astronomy University of California Los Angeles California 90095 USA and Instituut-Lorentz/LION Universiteit Leiden 2300 RA Leiden The Netherlands

DNA condensation in vivo relies on electrostatic complexation with small cations or large histones. We report a synchrotron x-ray study of the phase behavior of DNA complexed with synthetic cationic dendrimers of intermediate size and charge. We encounter unexpected structural transitions between columnar mesophases with in-plane square and hexagonal symmetries, as well as liquidlike disorder. The isoelectric point is a locus of structural instability. A simple model is proposed based on competing long-range electrostatic interactions and short-range entropic adhesion by counterion release.

关键词： .short-range complexation columnar counterion mesophases DNA condensation spermidine histones

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Coiling instabilities of multilamellar tubes

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Physical Review E 2002年第6期66卷 061501-061501页

作者： C. D. Santangelo P. Pincus Department of Physics University of California Santa Barbara California 93106 Department of Materials University of California Santa Barbara California 93106 Program in Biomolecular Science and Engineering University of California Santa Barbara California 93106

Myelin figures are densely packed stacks of coaxial cylindrical bilayers that are unstable to the formation of coils or double helices. These myelin figures appear to have no intrinsic chirality. We show that such cylindrical membrane stacks can develop an instability when they acquire a spontaneous curvature or when the equilibrium distance between membranes is decreased. This instability breaks the chiral symmetry of the stack and may result in coiling. A unilamellar cylindrical vesicle, on the other hand, will develop an axisymmetric instability, possibly related to the pearling instability.

关键词： Tubes (components)

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Material Anisotropy Revealed by Phase Contrast in Intermittent Contact Atomic Force Microscopy

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Physical Review Letters 2002年第22期88卷 226103-226103页

作者： Matthew S. Marcus Robert W. Carpick Darryl Y. Sasaki M. A. Eriksson Physics Department University of Wisconsin–Madison Madison Wisconsin 53706-1390 Department of Engineering Physics Materials Science Program and Rheology Research Center University of Wisconsin–Madison Madison Wisconsin 53706-1687 Biomolecular Materials and Interface Science Department Sandia National Laboratories Albuquerque New Mexico 87185-1413

Phase contrast in intermittent-contact atomic force microscopy (AFM) reveals in-plane structural and mechanical properties of polymer monolayers. This is surprising, because measurements of nanoscale in-plane properties typically require contact mode microscopies. Our measurements are possible because the tip oscillates not just perpendicular but also parallel to the sample surface along the long axis of the cantilever. This lateral tip displacement is virtually universal in AFM, implying that any oscillating-tip AFM technique is sensitive to in-plane material properties.

关键词： .anisotropic perpendicular Atomic force anisotropy phase contrast monolayers cantilever Tip-sample in-plane properties rotational symmetry long axis

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Cu/Zn- and Mn-superoxide dismutases are specifically up-regulated in neurons after focal brain injury

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Developmental Neurobiology 2000年第1期45卷

作者： Akihide Takeuchi Osamu Miyaishi Kazutoshi Kiuchi Ken-ichi Isobe Department of Basic Gerontology National Institute for Longevity Sciences 36-3 Gengo Morioka-cho Oobu 474-8522 Japan Laboratory for Genes of Motor Systems Bio-Mimetic Control Research Program RIKEN 2271-130 Anagahora Shimoshidami Moriyama-ku Nagoya 463-0003 Japan Department of Biomolecular Science Faculty of Engineering Gifu University 1-1 Yanagido Gifu 501-1193 Japan

In previous studies, we have demonstrated that damaged neurons within a boundary area around necrosis fall into delayed cell death due to the cytotoxic effect of microglial nitric oxide (NO), and are finally eliminated by activated microglia. In contrast, neurons in a narrow surrounding region nearby this boundary area remain alive even though they may encounter cytotoxic NO. To investigate the mechanism by which neurons tolerate this oxidative stress, we examined the in vitro and in vivo expression levels of superoxide dismutase (SOD) under pathological conditions. Results from our in situ hybridization and immunohistochemical studies showed up-regulation of Cu/Zn-SOD only in neurons outside the boundary area, whereas up-regulation of Mn-SOD was detected in both neurons and glial cells in the same region. In vitro experiments using rat PC12 pheochromocytoma and C6 glioma cell lines showed that induction of both Cu/Zn- and Mn-SOD mRNA could only be detected in PC12 cells after treatment with NO donors, while a slight induction of Mn-SOD mRNA alone could be seen in C6 glioma cells. The mechanism of resistance toward oxidative stress therefore appears to be quite different between neuronal and glial cells. It is assumed that these two types of SOD might play a critical role in protecting neurons from NO cytotoxicity in vivo, and the inability of SOD induction in damaged neurons seems to cause their selective elimination after focal brain injury. © 2000 John Wiley & Sons, Inc. J Neurobiol 45: 39–46, 2000

关键词： superoxide dismutase neuronal damage free radicals PC12 cells C6 cells

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Contributory presentations/posters

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Journal of Biosciences 1999年第1期24卷 33-198页

作者： N. Manoj V. R. Srinivas A. Surolia M. Vijayan K. Suguna R. Ravishankar R. Schwarzenbacher K. Zeth Diederichs G. M. Kostner A. Gries P. Laggner R. Prassl Madhusudan Pearl Akamine Nguyen-huu Xuong Susan S. Taylor M. Bidva Sagar K. Saikrishnan S. Roy K. Purnapatre P. Handa U. Varshney B. K. Biswal N. Sukumar J. K. Mohana Rao A. Johnson Vasantha Pattabhi S. Sri Krishna Mira Sastri H. S. Savithri M. R. N. Murthy Bindu Pillai Kannan M. V. Hosur Mukesh Kumar Swati Patwardhan K. K. Kannan B. Padmanabhaa S. Sasaki-Sugio M. Nukaga T. Matsuzaki S. Karthikevan S. Sharma A. K. Sharma M. Paramasivam P. Kumar J. A. Khan S. Yadav A. Srinivasan T. P. Singh S. Gourinath Neelima Alam A. Srintvasan Vikas Chandra Punit Kaur Ch. Betzel S. Ghosh A. K. Bera S. Bhattacharya S. Chakraborty A. K. Pal B. P. Mukhopadhyay I. Dey U. Haldar Asok Baneriee Jozef Sevcik Adriana Solovicova K. Sekar M. Sundaralingam N. Genov Dong-cai Liang Tao Jiang Ji-ping Zhang Wen-rui Chang Wolfgang Jahnke Marcel Blommers S. C. Panchal R. V. Hosur Bindu Pillay Puniti Mathur S. Srivatsun Ratan Mani Joshi N. R. Jaganathan V. S. Chauhan H. S. Atreya S. C. Sahu K. V. R. Chary Girjesh Govil Elisabeth Adjadj Éric Quinjou Nadia Izadi-Pruneyre Yves Blouquit Joël Mispelter Bernadette Heyd Guilhem Lerat Philippe Milnard Michel Desmadreil Y. Lin B. D. Nageswara Rao Vidva Raghunathan Mei H. Chau Prashant Pesais Sudha Srivastava Evans Coutinho Anil Saran Leizl F. Sapico Jayson Gesme Herbert Lijima Raymond Paxton Thamarapu Srikrishnan C. R. Grace G. Nagenagowda A. M. Lynn Sudha M. Cowsik Sarata C. Sahu S. Chauhan A. Bhattacharya G. Govil Anil Kumar Maurizio Pellecchia Erik R. P. Zuiderweg Keiichi Kawano Tomoyasu Aizawa Naoki Fujitani Yoichi Hayakawa Atsushi Ohnishi Tadayasu Ohkubo Yasuhiro Kumaki Kunio Hikichi Katsutoshi Nitta V. Rani Parvathy R. M. Kini Takumi Koshiba Yoshihiro Kobashigawa Min Yao Makoto Demura Astushi Nakagawa Isao Tanaka Kunihiro Kuwajima Jens Linge Seán O. Donoghue Michael Nilges G. Chakshusmathi Girish S. Ratnaparkhi P. K. Madhu R. Varadarajan C. Tetreau Molecular Biophysics Unit Indian Institute of Science Bangalore India Austrian Academy of Sciences Institute of Biophysics and X-ray Structure Research Graz Austria Faculty of Biology University of Konstanz Germany Institute of Medical Biochemistry University of Graz Austria Howard Huges Medical Institute Department of Chemistry & Biochemistry University of California La Jolla USA Department of Chemistry & Biochemistry University of California San Diego La Jolla USA Molecular Biophysics Unit India Department of Microbiology &Cell Biology Indian Institute of Science Bangalore India Macromolecular Structure Laboratory NCI - Frederick Cancer Research and Development Center ABL - Basic Research Program Frederick USA Department of Crystallography and Biophysics University of Madras Chennai Biochemistry Department Indian Institute of Science Bangalore India Condensed Matter Physics Division B.A.R.C. Trombay Mumbai Condensed Matter Physics Division Bhabha Atomic Research Centre Trombay Mumbai IMCB The University of Tokyo Tokyo Japan Mitsubishi Chemical Corporation Yokohama Research Center Yokohama Japan Faculty of Pharmaceutical Sciences Chiba University Chiba Japan Department of Biophysics All India Institute of Medical Sciences New Delhi India Department of Biophysics All India Institute of Medical sciences New Delhi India Institüt Physiologische Chemie Hamburg Germany Biophysics Department Bose Institute Calcutta India Slovak Academy of Sciences Institute of Molecular Biology Bratislava Slovakia Indian Institute of Science Bioinformatics Centre Bangalore Departments of Chemistry and Biochemistry Biological Macromolecular Structure Center USA Bulgarian Academy of Sciences Institute of Organic Chemistry Sofia Bulgaria Chinese Academy of Sciences Institute of Biophysics Beijing China Novartis Pharma AG Preclinical Research Basel Switzerland Department of Chemical Sciences Tata Institute of Fundamental Research Mumbai India Solid State Physics Div

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Membrane-based displacement flow immunoassay

Membrane-based displacement flow immunoassay

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Annual International Conference of the IEEE engineering in Medicine and Biology Society (EMBC)

作者： S.Y. Rabbany L.M. Pritsiolas W.A. Marganski A.W. Kusterbeck F.S. Ligler Bioengineering Program Hofstra University Hempstead NY USA Naval Research Laboratory Center for Biomolecular Science and Engineering Washington D.C. DC USA

A continuous flow displacement immunoassay has been developed in order to detect nanomolar quantities of two explosives (TNT and RDX). Antibodies are immobilized onto a porous membrane with surface reactive sites designed to facilitate the covalent binding of the antibody. Having saturated the immobilized antibody with labeled antigen, the target analyte is introduced and the displacement reactions are monitored using a fluorimeter. The displaced labeled antigen detected is proportional to the concentration of the analyte introduced into the column. Multiple assays were performed using columns containing individual membranes. Sensitivity limits were in the low nanomolar range.

关键词： Immune system Biomembranes Fluorescence Explosives Monitoring Phased arrays Signal generators Biomedical engineering Laboratories Molecular biophysics

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Physical sciences and engineering Advances in Life sciences and Oncology 1

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丛书名： science Policy Reports

1000年

作者： Paul Janmey Daniel Fletcher Sharon Gerecht Ross Levine Parag Mallick Owen McCarty Lance Munn Cynthia Reinhart-King

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Mechanism-Driven Design of Multispecific Antibodies for Targeted Disease Treatment

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Chemical and biomolecular engineering 1000年第1期15卷 105-138页

作者： Justyn Fine Bunyarit Meksiriporn Jiacheng Tan Jamie B. Spangler 2Translational Tissue Engineering Center Johns Hopkins University School of Medicine Baltimore Maryland USA email: jamie.spangler@jhu.edu 1Program in Molecular Biophysics Johns Hopkins University Baltimore Maryland USA 4Department of Biology School of Science King Mongkut's Institute of Technology Ladkrabang Bangkok Thailand 3Department of Biomedical Engineering Johns Hopkins University School of Medicine Baltimore Maryland USA 5Department of Chemical & Biomolecular Engineering Johns Hopkins University School of Engineering Baltimore Maryland USA 7Department of Molecular Microbiology and Immunology Johns Hopkins University Bloomberg School of Public Health Baltimore Maryland USA 6Departments of Oncology Opthalmology and Molecular Microbiology and Immunology Bloomberg-Kimmel Institute for Cancer Immunotherapy and Sidney Kimmel Comprehensive Cancer Center Johns Hopkins University School of Medicine Baltimore Maryland USA

Antibody-based therapeutics constitute a rapidly growing class of pharmaceutical compounds. However, monoclonal antibodies, which specifically engage only one target, often lack the mechanistic intricacy to treat complex diseases. To expand the utility of antibody therapies, significant efforts have been invested in designing multispecific antibodies, which engage multiple targets using a single molecule. These efforts have culminated in remarkable translational progress, including nine US Food and Drug Administration–approved multispecific antibodies, with countless others in various stages of preclinical or clinical development. In this review, we discuss several categories of multispecific antibodies that have achieved clinical approval or shown promise in earlier stages of development. We focus on the molecular mechanisms used by multispecific antibodies and how these mechanisms inform their customized design and formulation. In particular, we discuss multispecific antibodies that target multiple disease markers, multiparatopic antibodies, and immune-interfacing antibodies. Overall, these innovative multispecific antibody designs are fueling exciting advances across the immunotherapeutic landscape.

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