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8 CONTENTS 0-8493-1141-1/02/$0.00+$1.50 © 2002 by CRC Press LLC Interactions of Cell- Penetrating Peptides with Membranes Laurent Chaloin, Nicole Van Mau, Gilles Divita, and Frédéric Heitz 8.1 Introduction ..................................................................................................164 8.2 Structural Determinations ............................................................................165 8.2.1 Analytical Methods: Conformational Identifications ......................166 8.2.1.1 NMR .................................................................................166 8.2.1.2 Circular Dichroism (CD)..................................................167 8.2.1.3 Fourier Transform InfraRed Spectroscopy (FTIR) ..........167 8.2.1.4 Diffraction.........................................................................168 8.2.2 Interactions with Phospholipids and Their Consequences..............168 8.2.2.1 The Monolayer Approach.................................................168 8.2.2.2 Lipid-Free Air–Water Interface ........................................168 8.2.2.3 Lipid-Containing Air–Water Interface..............................169 8.2.2.4 Bilayers .............................................................................169 8.2.2.5 Fluorescence .....................................................................169 8.2.2.6 Electron Paramagnetic Resonance (EPR) Spectroscopy .....................................................................170 8.2.2.7 Atomic Force Microscopy (AFM) ...................................170 8.2.2.8 An Example of Multidisciplinary Approach Based on Monolayers ..................................................................170 8.2.2.8.1 Monolayer Study ............................................171 8.2.2.8.2 Influence of the Sequence ..............................175 8.3 Cellular Internalization of Antennapedia.....................................................177 8.4 Internalization via a Vesicular Process ........................................................177 8.5 Internalization via Receptor.........................................................................177 8.6 Unfolding for Conjugate CPP–Protein........................................................179 8.7 Origin of the Toxicity ..................................................................................179 8.8 Conclusions and Perspectives ......................................................................180 References..............................................................................................................181 163
164 Cell-Penetrating Peptides: Processes and Applications 8.1 INTRODUCTION Cellular uptake of therapeutic agents requires assistance of agents facilitating the crossing of the natural barrier, which is the plasma membrane. A large number of such agents have been developed in the recent past, mainly devoted to the transfer of nucleic acids and proteins. Among them, peptides appear to be very powerful tools for the transfer of DNAs; two main strategies are concerned: (1) covalent linkage between cargo and vector, thus forming a conjugate, and (2) formation of a complex between the two partners. Within the peptides used in the first strategy, the first efficient vector developed is polylysine, which can act as vector for oligonucleotides. 1-5 Later, more sophisticated molecules such as the L-oligomers were proposed as vectors of cytotoxic agents with the aim to develop an anticancer strategy. 6,7 Simultaneously, fusion peptides 8 and peptides based on the KDEL sequence 9,10 were proposed as efficient vectors in the antisense strategy. Although still based on peptide sequences, vectors issued from the homeodomain of Antennapedia were shown to translocate toward the nuclei of nervous cells in culture. 11-15 This α-helical peptide appears to be a very powerful agent, facilitating membrane crossing for both peptides 16,17 and oligonucleotides. 18 These properties led to a wider search for other translocating peptide sequences; among them, the so-called Tat-derived peptides from HIV1 were found. 19-21 Also, other peptides derived from natural sequences have been proposed. These are a peptide-based on neuropeptide Y, 22 shown to be an efficient vector for daunorubicin and doxorubicin although it requires the presence of a receptor, and a peptide issued from human calcitonin that acts through excised bovine nasal mucosa. 23 As to the second strategy that involves the formation of complexes, besides the well documented approaches based on viruses, 24-27 liposomes, 28 cationic lipids, 29 or PEI, 30 peptidic vectors have also been investigated. All of them share the common presence of cationic residues, but differ mainly from each other by distribution of the basic residues along the peptide chain and thus by their ability to form an amphipathic structure. 31-42 According to the conformation involved in the formation of the amphipathic structure, these vectors are able to translocate charged molecules such as DNA or hydrophobic drugs. All these peptides are short (below 40 residues) and constitute a series of vectors which validate the peptide approach. However, none of the peptidic vectors reported so far can be considered perfect. In order to attempt and define a new generation of nontoxic vector peptides with specific targeting, a prerequisite is to identify the mechanism leading to the cellular internalization process of vectors in the free form and when associated with the cargo. Two main processes with different mechanisms leading to cellular internalization must be examined: through the endosome pathway or by direct penetration into the cytoplasm. In both cases, an obligatory step in such an approach is devoted to structural investigations for identification of structural requirements and their optimization for design of efficient vectors. The cellular internalization mechanism can be summarized as a three-step process; (1) uptake by the cellular membrane, (2) translocation through the membrane, and (3) release on the cytoplasmic side into the cell interior.
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CELL- PENETRATING PEPTIDES Processe
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Pharmacology and Toxicology: Basic
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Library of Congress Cataloging-in-P
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to the handbook are prominent resea
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REFERENCES 1. Green, M. and Loewens
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Contributors Mats Andersson Microbi
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Erin T. Pelkey Department of Chemis
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Contents Section I Classes of Cell-
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Chapter 16 Cell-Penetrating Peptide
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The Tat-Derived Cell-Penetrating Pe
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24 Cell-Penetrating Peptides: Proce
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3 Transportans Margus Pooga, Mattia
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Transportans 55 Indeed, galparan is
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Transportans 57 especially the endo
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Transportans 59 In the penetration
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Transportans 61 A 21-mer antisense
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Transportans 63 Commonly, the prote
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Transportans 65 antibiotin antibodi
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Transportans 67 For cross-linking o
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Transportans 69 and still retain ef
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Model Amphipathic Peptides 73 its D
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Model Amphipathic Peptides 75 pmol/
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TABLE 4.1 Internalization of Peptid
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TABLE 4.2 Internalization of Peptid
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Model Amphipathic Peptides 81 relat
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Model Amphipathic Peptides 87 A cat
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Model Amphipathic Peptides 89 At th
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Model Amphipathic Peptides 91 16. H
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Signal Sequence-Based Cell-Penetrat
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Structure Prediction of CPPs and It
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Biophysical Studies of Cell-Penetra
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Toxicity and Side Effects of Cell-P
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264 Cell-Penetrating Peptides: Proc
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Kinetics of Uptake of Cell-Penetrat
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Cell-Penetrating Peptide Conjugatio
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FIGURE 15.9 (Color Figure 15.9 foll
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Cell-Penetrating Peptides as Vector
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TABLE 16.1 Examples of Transport of
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CPP 2 Cargo or mRNA CAP Antisense A
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Microbial Membrane-Permeating Pepti
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Index A Abaecin, 129 Abz radiolabel
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Index 399 Diffraction, 168 Disulphi
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Index 401 structure prediction, 187
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Index 403 pRB proteins, Tat-E1A bin
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Index 405 lipid perturbation (secon
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