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Life at the nanoscale : atomic force microscopy of live cells PDF

444 Pages·2011·9.64 MB·English
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Life at the Nanoscale Contents.indd i 5/12/2011 4:14:56 PM Published by ƒ–ƒˆ‘”†—„Ž‹•Š‹‰–‡Ǥ–†Ǥ ‡–Š‘—•‡‡˜‡Žǡ—–‡…‘™‡”͵ ͺ‡ƒ•‡‘—Ž‡˜ƒ”† ‹‰ƒ’‘”‡Ͳ͵ͺͻͺͺ ƒ‹Žǣ‡†‹–‘”‹ƒŽ̷’ƒ•–ƒˆ‘”†Ǥ…‘ ‡„ǣ™™™Ǥ’ƒ•–ƒˆ‘”†Ǥ…‘ British Library Cataloguing-in-Publication Data …ƒ–ƒŽ‘‰—‡”‡…‘”†ˆ‘”–Š‹•„‘‘‹•ƒ˜ƒ‹Žƒ„Ž‡ˆ”‘–Š‡”‹–‹•Š‹„”ƒ”›Ǥ Life at the Nanoscale: Atomic Force Microscopy of Live Cells ‘’›”‹‰Š–̹ʹͲͳͳ„›ƒ–ƒˆ‘”†—„Ž‹•Š‹‰–‡Ǥ–†Ǥ All rights reserved. This book, or parts thereof, may not be reproduced in any form or by any means, electronic or mechanical, including photocopying, recording or any information storage and retrieval system now known or to be invented, without written permission from the publisher. ‘”’Š‘–‘…‘’›‹‰‘ˆƒ–‡”‹ƒŽ‹–Š‹•˜‘Ž—‡ǡ’Ž‡ƒ•‡’ƒ›ƒ…‘’›‹‰ˆ‡‡–Š”‘—‰Š–Š‡ ‘’›”‹‰Š–Ž‡ƒ”ƒ…‡‡–‡”ǡ…Ǥǡʹʹʹ‘•‡™‘‘†”‹˜‡ǡƒ˜‡”•ǡͲͳͻʹ͵ǡǤ –Š‹•…ƒ•‡’‡”‹••‹‘–‘’Š‘–‘…‘’›‹•‘–”‡“—‹”‡†ˆ”‘–Š‡’—„Ž‹•Š‡”Ǥ ͻ͹ͺǦͻͺͳǦͶʹ͸͹Ǧͻ͸ǦͲȋƒ”†…‘˜‡”Ȍ ͻ͹ͺǦͻͺͳǦͶʹ͸͹Ǧͻ͹Ǧ͹ȋ‡‘‘Ȍ ”‹–‡†‹‹‰ƒ’‘”‡ Contents.indd iv 5/12/2011 4:15:11 PM Contents Preface vi Chapter 1 Observing the Nanoscale Organization of Model 1 Biological Membranes by Atomic Force Microscopy Pierre-Emmanuel Milhiet and Christian Le Grimellec Chapter 2 High-Resolution Atomic Force Microscopy of Native 21 Membranes Nikohy Buzhynskyy, Lu-Ning Liu, Ignacio Casuso and Simon Scheuring Chapter 3 Microbial Cel Imaging Using Atomic Force Microscopy 45 Mitchel J. Doktycz, Claretta J. Sullivan, Ninell Pollas Mortensen and David P. Allison Chapter 4 Resolving the High-Resolution Architecture, Asembly 71 and Functional Repertoire of Bacterial Systems by in vitro Atomic Force Microscopy Alexander J. Malkin Chapter 5 Understanding Cel Secretion and Membrane Fusion 9 Processes on the Nanoscale Using the Atomic Force Microscope Bhanu P. Jena Chapter 6 Nanophysiology of Cels, Chanels and Nuclear Pores 17 Hermann Schillers, Hans Oberleithner and Victor Shahin Chapter 7 Topography and Recognition Imaging of Cels 145 Lilia Chtcheglova, Linda Wildling and Peter Hinterdorfer Chapter 8 High-Sped Atomic Force Microscopy for Dynamic 163 Biological Imaging Takayuki Uchihashi and Toshio Ando Chapter 9 Near-Field Scaning Optical Microscopy of Biological 185 Membranes Thomas S. van Zanten and Maria F. Garcia-Parajo Chapter 10 Quantifying Cel Adhesion Using Single-Cel Force 209 Spectroscopy Anna Taubenberger, Jens Friedrichs and Daniel J. Mutter vi Contents Chapter 11 Probing Celular Adhesion at the Single-Molecule Level 225 Félix Rico, Xiaohui Zhang and Vincent T. Moy Chapter 12 Mapping Membrane Proteins on Living Cels Using the 263 Atomic Force Microscope Atsushi Ikai and Rehana Afrin Chapter 13 Probing Bacterial Adhesion Using Force Spectroscopy 285 Terri A. Camesano Chapter 14 Force Spectroscopy of Mineral-Microbe Bonds 301 Brian H. Lower and Steven K. Lower Chapter 15 Single-Molecule Force Spectroscopy of Microbial Cel 317 Envelope Proteins Claire Verbelen, Vincent Dupres, David Alsteens, Guillaume Andre and Yves F. Dufrêne Chapter 16 Probing the Nanomechanical Properties of Viruses, 35 Cells and Cellular Structures Sandor Kasas and Giovanni Dietler Chapter 17 Label-Fre Monitoring of Cel Signaling Proceses 353 Through AFM-Based Force Measurements Charles M. Cuerrier, Elie Simard, Charles-Antoine Lamontagne, Julie Boucher, Yannick Miron and Michel Grandbois Chapter 18 Investigating Mammalian Cel Nanomechanics with 375 Simultaneous Optical and Atomic Force Microscopy Yaron R. Silberberg, Louise Guolla and Andrew E. Felling Chapter 19 The Role of Atomic Force Microscopy in Advancing 405 Diatom Research into the Nanotechnology Era Michael]. Higgins and Richard Wetherbee Chapter 20 Atomic Force Microscopy for Medicine 421 Shivani Sharma and James K. Gimzewski Index 437 Preface ––Š‡…”‘••”‘ƒ†•‘ˆŽ‹ˆ‡•…‹‡…‡•ƒ†ƒ‘–‡…Š‘Ž‘‰›ǡ–Š‡ƒ‘•…ƒŽ‡ƒƒŽ›•‹• ‘ˆŽ‹˜‹‰…‡ŽŽ•„›ƒ–‘‹…ˆ‘”…‡‹…”‘•…‘’›ȋ Ȍ‹•ƒ‡š…‹–‹‰ǡ”ƒ’‹†Ž›‡˜‘Ž˜‹‰ ”‡•‡ƒ”…Šϐ‹‡Ž†Ǥ‹–Š‹–•ƒ„‹Ž‹–›–‘‘„•‡”˜‡ƒ†ˆ‘”…‡’”‘„‡…‡ŽŽ•ƒ†„‹‘Ž‘‰‹…ƒŽ ‡„”ƒ‡• –‘ ‘Ž‡…—Žƒ” ”‡•‘Ž—–‹‘ ƒ† —†‡” ’Š›•‹‘Ž‘‰‹…ƒŽ…‘†‹–‹‘•ǡ ‘ơ‡”•ƒ™‡ƒŽ–Š‘ˆ‡™‘’’‘”–—‹–‹‡•‹„‹‘Ž‘‰›ƒ†‡†‹…‹‡ǤŠƒ–‹• –Š‡ƒ‘•…ƒŽ‡‘”‰ƒ‹œƒ–‹‘‘ˆ„‹‘Ž‘‰‹…ƒŽ‡„”ƒ‡•ǫ‘™†‘…‡ŽŽ•—”ˆƒ…‡• ”‡‘†‡Ž †—”‹‰…‡ŽŽ ‰”‘™–Š ‘” ‹…—„ƒ–‹‘™‹–Š †”—‰•ǫŠƒ– ‹• –Š‡ •’ƒ–‹ƒŽ †‹•–”‹„—–‹‘‘ˆ…‡ŽŽ•—”ˆƒ…‡”‡…‡’–‘”•ǫŠƒ–ƒ”‡–Š‡ˆ‘”…‡•†”‹˜‹‰…‡ŽŽƒ†Š‡•‹‘ ’”‘…‡••‡•ǫŠƒ–ƒ”‡–Š‡ƒ†Š‡•‹˜‡ƒ†‡…Šƒ‹…ƒŽ’”‘’‡”–‹‡•‘ˆ…‡ŽŽ•ƒ†‘ˆ –Š‡‹”‹†‹˜‹†—ƒŽ…‘•–‹–—‡–•ǡƒ†Š‘™ƒ”‡–Š‡›”‡Žƒ–‡†–‘ˆ—…–‹‘ǫŠ‡•‡ƒ”‡ •‘‡‘ˆ–Š‡’‡”–‹‡–“—‡•–‹‘•–Šƒ–…ƒ‘™„‡ƒ††”‡••‡†„› ǡ–Š‡”‡„› …‘–”‹„—–‹‰ –‘ ‹’”‘˜‹‰ ‘—” —†‡”•–ƒ†‹‰ ‘ˆ –Š‡ •–”—…–—”‡Ȃˆ—…–‹‘ ”‡Žƒ–‹‘•Š‹’•‘ˆ…‡ŽŽ‡„”ƒ‡•ƒ†…‡ŽŽ™ƒŽŽ•Ǥ Š‹•„‘‘’”‘˜‹†‡•ƒ‘˜‡”˜‹‡™‘ˆ–Š‡—•‡‘ˆ ƒ†”‡Žƒ–‡†–‡…Š‹“—‡• ˆ‘”…‡ŽŽ ƒƒŽ›•‹•ǡ ‰‘‹‰ ˆ”‘ –Š‡ „ƒ•‹… ’”‹…‹’Ž‡• –‘ –Š‡ ƒ’’Ž‹…ƒ–‹‘•Ǥ Š‡ †‹ơ‡”‡–…Šƒ’–‡”•ǡ ƒŽŽ ™”‹––‡ „› Ž‡ƒ†‹‰ ‡š’‡”–• ‹ –Š‡‹” ϐ‹‡Ž†ǡ…‘˜‡” ‡–Š‘†‘Ž‘‰‹‡•ˆ‘”’”‡’ƒ”‹‰ƒ†ƒƒŽ›œ‹‰‡„”ƒ‡•ƒ†…‡ŽŽ•‘ˆƒŽŽ‹†•ǡ †‹•…—••–Š‡’”‹…‹’Ž‡•‘ˆƒ†˜ƒ…‡† ‘†ƒŽ‹–‹‡•ǡ‹…Ž—†‹‰Š‹‰ŠǦ”‡•‘Ž—–‹‘ ‹ƒ‰‹‰ǡ Š‹‰ŠǦ•’‡‡† ‹ƒ‰‹‰ǡ ”‡…‘‰‹–‹‘ ‹ƒ‰‹‰ǡ •‹‰Ž‡Ǧ‘Ž‡…—Ž‡ ƒ† •‹‰Ž‡Ǧ…‡ŽŽ ˆ‘”…‡ •’‡…–”‘•…‘’›ǡ ‡…Šƒ‹…ƒŽ ‡ƒ•—”‡‡–•ǡ ƒ† Š‹‰ŠŽ‹‰Š–• ”‡…‡–ƒ’’Ž‹…ƒ–‹‘•‹ƒ˜ƒ”‹‡–›‘ˆϐ‹‡Ž†•ǡ‹…Ž—†‹‰…‡ŽŽ„‹‘Ž‘‰›ǡ‹…”‘„‹‘Ž‘‰›ǡ „‹‘’Š›•‹…•ǡ•–”—…–—”ƒŽ„‹‘Ž‘‰›ǡ’Š›•‹‘Ž‘‰›ƒ†‡†‹…‹‡Ǥ Š‡ϐ‹”•–•‡…–‹‘‘ˆ–Š‡„‘‘…‘˜‡”•”‡…‡–’”‘‰”‡••‹‹ƒ‰‹‰…‡ŽŽ•ƒ† ‡„”ƒ‡•—•‹‰ ƒ†”‡Žƒ–‡†•…ƒ‹‰’”‘„‡•Ǥ…Šƒ’–‡”ͳǡ‹ŽŠ‹‡–ƒ† ‡ ”‹‡ŽŽ‡…‡š’Ž‘”‡–Š‡ƒ‘•…ƒŽ‡‘”‰ƒ‹œƒ–‹‘‘ˆ•—’’‘”–‡†Ž‹’‹†„‹Žƒ›‡”•ǡ ™‹–Š ƒ ‡’Šƒ•‹• ‘ Ž‹’‹† ‹…”‘†‘ƒ‹• ƒ† ‡„”ƒ‡ ’”‘–‡‹•Ǥ Š‡ …‘–”‹„—–‹‘„›–Š‡…Š‡—”‹‰–‡ƒȋ…Šƒ’–‡”ʹȌ†‡‘•–”ƒ–‡•–Š‡’‘™‡”‘ˆ Š‹‰ŠǦ”‡•‘Ž—–‹‘ ‹ƒ‰‹‰ˆ‘””‡•‘Ž˜‹‰–Š‡•—’”ƒ‘Ž‡…—Žƒ”ƒ”…Š‹–‡…–—”‡ ‘ˆƒ–‹˜‡‡„”ƒ‡•Ǥ‘–›…œet al. ȋ…Šƒ’–‡”͵Ȍ”‡˜‹‡™–Š‡—•‡‘ˆ ˆ‘” ‹…”‘„‹ƒŽ…‡ŽŽ‹ƒ‰‹‰ǡˆ‘…—•‹‰‘•ƒ’Ž‡’”‡’ƒ”ƒ–‹‘ƒ†‹ƒ‰‹‰…‘†‹–‹‘•ǡ ƒ†’”‘˜‹†‹‰˜ƒ”‹‘—•‡šƒ’Ž‡•‘ˆƒ’’Ž‹…ƒ–‹‘•‹‹…”‘„‹‘Ž‘‰›Ǥ…Šƒ’–‡”Ͷǡ ƒŽ‹†‡•…”‹„‡•–Š‡—‹“—‡…ƒ’ƒ„‹Ž‹–‹‡•‘ˆ ˆ‘”’”‘„‹‰–Š‡ƒ”…Š‹–‡…–—”‡ǡ ƒ••‡„Ž› ƒ††›ƒ‹…• ‘ˆ „ƒ…–‡”‹ƒŽ •—”ˆƒ…‡•Ǥ ‡ƒ ȋ…Šƒ’–‡” ͷȌ •Š‘™•Š‘™ …ƒŠ‡Ž’—•—†‡”•–ƒ†…‡ŽŽ•‡…”‡–‹‘ƒ†‡„”ƒ‡ˆ—•‹‘’”‘…‡••‡• Contents.indd vii 5/12/2011 4:15:13 PM viii Preface ‘ –Š‡ ƒ‘•…ƒŽ‡Ǥ Schillers et al. ȋ…Šƒ’–‡” ͸Ȍ •—”˜‡› –Š‡ ‡‡”‰‹‰ ϐ‹‡Ž† ‘ˆ ƒ‘’Š›•‹‘Ž‘‰›ǡ•Š‘™‹‰Š‘™ ’”‘˜‹†‡•‡™‹•‹‰Š–•‹–‘–Š‡†›ƒ‹…• ‘ˆ’”‘–‡‹•‹’Žƒ•ƒ‡„”ƒ‡•ǡ‹–‘–Š‡‡„”ƒ‡mechanodynamics of vascular endothelial cells and into the structural and physical ’”‘’‡”–‹‡• ‘ˆ–Š‡—…Ž‡ƒ”‡˜‡Ž‘’‡ǤŠ‡Žƒ•––Š”‡‡…‘–”‹„—–‹‘•‘ˆ–Š‡•‡…–‹‘†‡ƒŽ™‹–Š ƒ†˜ƒ…‡†‹ƒ‰‹‰‘†ƒŽ‹–‹‡•ǤŠ–…Š‡‰Ž‘˜ƒ et al. ȋ…Šƒ’–‡”͹Ȍϐ‹”•–†‡•…”‹„‡–Š‡ „ƒ•‹…•‘ˆƒ”‡…‡– ‹ƒ‰‹‰‘†‡ƒ‡†Dz•‹—Ž–ƒ‡‘—•–‘’‘‰”ƒ’Š›ƒ† ”‡…‘‰‹–‹‘‹ƒ‰‹‰dzƒ†‹–•ƒ’’Ž‹…ƒ–‹‘ˆ‘”ƒ’’‹‰…‡ŽŽ•—”ˆƒ…‡”‡…‡’–‘”•Ǥ …Š‹Šƒ•Š‹ ƒ† †‘ ȋ…Šƒ’–‡” ͺȌ ‡š– †‡‘•–”ƒ–‡ Š‘™ Š‹‰ŠǦ•’‡‡† ‹ƒ‰‹‰ ‹• ”‡˜‘Ž—–‹‘‹œ‹‰ ‘—” ’‡”…‡’–‹‘ ‘ˆ †›ƒ‹… „‹‘Ž‘‰‹…ƒŽ ’”‘…‡••‡• ƒ††‹•…—•• –Š‡ ’‘–‡–‹ƒŽ ‘ˆ –Š‡‡–Š‘† ˆ‘” ‘„•‡”˜‹‰…‡ŽŽ‡„”ƒ‡•Ǥ –Š‡Žƒ•–…‘–”‹„—–‹‘ǡ˜ƒƒ–‡ƒ† ƒ”…‹ƒǦƒ”ƒŒ‘ ȋ…Šƒ’–‡”ͻȌˆ‘…—•‘–Š‡ —•‡‘ˆ‡ƒ”Ǧϐ‹‡Ž†•…ƒ‹‰‘’–‹…ƒŽ‹…”‘•…‘’›ˆ‘””‡•‘Ž˜‹‰–Š‡…Ž—•–‡”‹‰‘ˆ ‡„”ƒ‡”‡…‡’–‘”•Ǥ –Š‡•‡…‘†•‡…–‹‘‘ˆ–Š‡„‘‘ǡ Ǧ„ƒ•‡†ˆ‘”…‡•’‡…–”‘•…‘’›‹•—•‡† –‘“—ƒ–‹ˆ›…‡ŽŽ—Žƒ”‹–‡”ƒ…–‹‘•‘˜‡”•…ƒŽ‡•”ƒ‰‹‰ˆ”‘™Š‘Ž‡…‡ŽŽ•–‘•‹‰Ž‡ ‘Ž‡…—Ž‡•ǤòŽŽ‡”ƒ†…‘ŽŽ‡ƒ‰—‡•ȋ…Šƒ’–‡”ͳͲȌϐ‹”•–’”‡•‡–ƒ‘˜‡”˜‹‡™‘ˆ –Š‡—•‡‘ˆ•‹‰Ž‡Ǧ…‡ŽŽˆ‘”…‡•’‡…–”‘•…‘’›ˆ‘”“—ƒ–‹ˆ›‹‰…‡ŽŽƒ†Š‡•‹‘ˆ‘”…‡•Ǥ ‹…‘ et al. ȋ…Šƒ’–‡” ͳͳȌ –Š‡ •—”˜‡› •‹‰Ž‡Ǧ‘Ž‡…—Ž‡ ˆ‘”…‡ •’‡…–”‘•…‘’› ‡–Š‘†•ƒ†–Š‡‘”‹‡•ˆ‘”—†‡”•–ƒ†‹‰–Š‡„‹†‹‰•–”‡‰–Š‘ˆ…‡ŽŽƒ†Š‡•‹‘ ‘Ž‡…—Ž‡•Ǥ…Šƒ’–‡”ͳʹǡƒ‹ƒ†ˆ”‹†‡•…”‹„‡ƒ†˜ƒ…‡•‹–Š‡†‡–‡…–‹‘ ƒ† ƒ’’‹‰ ‘ˆ ‡„”ƒ‡ ’”‘–‡‹•Ǥ ‘˜‹‰ ‹–‘ –Š‡ ‹…”‘„‹ƒŽ ™‘”Ž†ǡ ƒ‡•ƒ‘ȋ…Šƒ’–‡”ͳ͵Ȍ‡š’Žƒ‹•Š‘™–‘‡ƒ•—”‡„ƒ…–‡”‹ƒŽ’‘Ž›‡”‡Žƒ•–‹…‹–› ƒ†„ƒ…–‡”‹ƒŽ‹–‡”ƒ…–‹‘•™‹–Šƒ ǡ™Š‹Ž‡‘™‡”ƒ†‘™‡”ȋ…Šƒ’–‡”ͳͶȌ ‡š’Ž‘”‡–Š‡ˆ‘”…‡•ƒ†„‘†•ƒ––Š‡‹–‡”ˆƒ…‡„‡–™‡‡‹…”‘‘”‰ƒ‹••ƒ† ‹‡”ƒŽ•Ǥ ‹ƒŽŽ›ǡ–Š‡—ˆ”²‡–‡ƒȋ…Šƒ’–‡”ͳͷȌ†‹•…—••‡•”‡…‡–’”‘‰”‡••‹ ‡ƒ•—”‹‰–Š‡ƒ†Š‡•‹˜‡ƒ†‡…Šƒ‹…ƒŽ’”‘’‡”–‹‡•‘ˆ‹…”‘„‹ƒŽ…‡ŽŽ‡˜‡Ž‘’‡ ’”‘–‡‹•Ǥ Š‡ Žƒ•– •‡…–‹‘ ‘ˆ –Š‡ ˜‘Ž—‡ ˆ‘…—•‡• ‘ Ǧ„ƒ•‡† ‡…Šƒ‹…ƒŽ ‡ƒ•—”‡‡–•Ǥ…Šƒ’–‡”ͳ͸ǡƒ•ƒ•ƒ†‹‡–Ž‡”’”‘˜‹†‡ƒ•Š‘”–‹–”‘†—…–‹‘ –‘ ‡Žƒ•–‹…‹–› ƒ† ‹†‡–ƒ–‹‘ ‡ƒ•—”‡‡–• ƒ† Š‹‰ŠŽ‹‰Š– ”‡Ž‡˜ƒ– ’—„Ž‹…ƒ–‹‘•‡š’Ž‘”‹‰–Š‡ƒ‘‡…Šƒ‹…ƒŽ’”‘’‡”–‹‡•‘ˆ„‹‘Ž‘‰‹…ƒŽ•›•–‡•ǡ ‹…Ž—†‹‰˜‹”—•‡•ƒ†…‡ŽŽ•Ǥ ”ƒ†„‘‹•ƒ†…‘ŽŽ‡ƒ‰—‡•ȋ…Šƒ’–‡”ͳ͹Ȍ…‘„‹‡ Ǧ„ƒ•‡†ˆ‘”…‡‡ƒ•—”‡‡–•™‹–ŠϐŽ—‘”‡•…‡…‡‹ƒ‰‹‰ˆ‘”–Š‡Žƒ„‡ŽǦˆ”‡‡ ‘‹–‘”‹‰‘ˆ…‡ŽŽ•‹‰ƒŽŽ‹‰’”‘…‡••‡•Ǥ…Šƒ’–‡”ͳͺǡ‡ŽŽ‹‰et al.—•‡ ƒ• ƒ –‘‘Ž –‘ †‡Ž‹˜‡” Ž‘…ƒŽ‹œ‡† ƒ‘‡…Šƒ‹…ƒŽ ˆ‘”…‡• –‘ Ž‹˜‹‰ ƒƒŽ‹ƒ …‡ŽŽ•ǡ™Š‹Ž‡‘’–‹…ƒŽŽ›‹ƒ‰‹‰„‹‘Ž‘‰‹…ƒŽ”‡•’‘•‡•ƒ––Š‡•‹‰Ž‡…‡ŽŽŽ‡˜‡ŽǤ –Š‡ƒŽ‰ƒ‡…‘–‡š–ǡ‹‰‰‹•ƒ†‡–Š‡”„‡‡ȋ…Šƒ’–‡”ͳͻȌ‡š’Žƒ‹–Š‡”‘Ž‡–Šƒ– Contents.indd viii 5/12/2011 4:15:14 PM Preface ix Šƒ•’Žƒ›‡†‹ƒ†˜ƒ…‹‰‘—”—†‡”•–ƒ†‹‰‘ˆ–Š‡‘”’Š‘‰‡‡•‹•ƒ† ‡…Šƒ‹…ƒŽ’”‘’‡”–‹‡•‘ˆ†‹ƒ–‘•Ǥ ‹ƒŽŽ›ǡŠƒ”ƒƒ† ‹œ‡™•‹ȋ…Šƒ’–‡” ʹͲȌ Š‹‰ŠŽ‹‰Š– –Š‡ ’‘–‡–‹ƒŽ ‘ˆ –‡…Š‹“—‡• ‹‡†‹…‹‡ǡ ’ƒ”–‹…—Žƒ”Ž› ‹ …ƒ…‡”†‹ƒ‰‘•–‹…•Ǥ Š‘’‡–Šƒ––Š‡„‘‘™‹ŽŽ‹–‡”‡•–•–—†‡–•ƒ†”‡•‡ƒ”…Š‡”•ˆ”‘˜ƒ”‹‘—• Š‘”‹œ‘•ǡ ™Š‡–Š‡” –Š‡› ƒ”‡ ‡™…‘‡”• ‘” ™‡ŽŽ –”ƒ‹‡† ‹ –Š‡ ϐ‹‡Ž†Ǥ Š‡ ˜‘Ž—‡•Š‘—Ž†Š‡Ž’–Š‡–‘‡˜ƒŽ—ƒ–‡–Š‡ƒ†˜ƒ–ƒ‰‡•ƒ†Ž‹‹–ƒ–‹‘•‘ˆ –‡…Š‹“—‡• ‹–Š‡‹”•’‡…‹ϐ‹… ϐ‹‡Ž†ƒ†–‘†‡ϐ‹‡ƒ’’”‘’”‹ƒ–‡’”‘…‡†—”‡•ƒ† …‘–”‘Ž• –Šƒ– ™‹ŽŽ Ž‡ƒ† –Š‡ –‘ •—……‡••ˆ—Ž ‡š’‡”‹‡–•Ǥ ƒ ’ƒ”–‹…—Žƒ”Ž› ‰”ƒ–‡ˆ—Ž–‘ƒŽŽƒ—–Š‘”•ˆ‘”–Š‡‹”‘—–•–ƒ†‹‰…‘–”‹„—–‹‘•ǡƒ†–‘’‡‘’Ž‡ƒ– ƒ–ƒˆ‘”†—„Ž‹•Š‹‰ˆ‘”–Š‡‹”‹˜ƒŽ—ƒ„Ž‡Š‡Ž’‹’—„Ž‹•Š‹‰–Š‡„‘‘Ǥ Yves Dufrêne Contents.indd ix 5/12/2011 4:15:14 PM Chapter 1 OBSERVING THE NANOSCALE ORGANIZATION OF MODEL BIOLOGICAL MEMBRANES BY ATOMIC FORCE MICROSCOPY Pierre-Emmanuel Milhiet and Christian Le Grimellec INSERM, Unité 554, Montpellier, France Université de Montpellier, CNRS, UMR 5048, Centre de Biochimie Structurale, Montpellier, France 2 Observing the Nanoscale OrganizaƟon of Model Biological Membranes In this complex context, artiϐicial membranes have been extensively used to mimic membrane organization, using either free-standing membranes like 4 liposomes or planar and supported model membranes. Giant unilamellar vesicles (GUVs) are very useful to study dynamic events and have been widely used to explore lipid domain formation using single-molecule optical 5 microscopy. However, this approach is restricted by diffraction-limited resolution and is therefore not suitable to probe membrane on the mesoscopic scale. Membranes supported on a solid support (supported lipid bilayer, or SLB) are very useful and robust systems that are compatible with most biophysical techniques, including ϐluorescence microscopy, ellipsometry and atomic force microscopy (AFM). The advantage of AFM, compared with other techniques, is the possibility to image, in real time, the topography of samples with nanometer lateral resolution. AFM, which consists in raster scanning of a sample surface with a sharp tip at the end of a soft cantilever, has been largely used for probing the two-dimensional (2D) organization of model membranes and for elucidating the mechanisms underlying lateral segregation of membrane constituents, especially membrane microdomain formation (for recent reviews see Refs. 6–8). Structural information of membrane proteins incorporated into SLBs with a subnanometer lateral resolution can also be obtained under conditions where proteins are tightly 9,10 packed. In this chapter, we describe the main strategies to prepare SLBs that are suitable for AFM analysis. After a brief methodological description of AFM imaging in liquid, we review major advances in the exploration of the topology of SLBs, focusing on the study of membrane microdomains and of membrane proteins. Progress in nanobiotechnology and recent technical developments that have improved the time and lateral resolution of AFM are also covered. 1.2 PREPARATION OF ARTIFICIAL SUPPORTED LIPID MEMBRANES Artiϐicial membranes are generally prepared on chemically inert, hydrophilic and flat solid supports, such as mica, highly oriented pyrolitic graphite, glass, silicon and gold. Different methods have been developed to prepare SLBs, but 11 the most popular technique, ϐirst described by McConnel’s group, remains the formation of supported membranes by fusion of large unilamellar lipid vesicles (LUVs) on a solid surface. LUVs are generally prepared via sonication or extrusion, and the vesicle solution is then added on top of the support. Vesicles then adsorb on the substrate before rupturing (Fig. 1.1). The composition of the buffer bathing the substrate has to be ϐinely tuned for allowing optimal

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