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Index 401<br />
structure prediction, 187–222<br />
toxicity, 245–261<br />
uptake kinetics, 277–293<br />
Melittin, 236–238, 240<br />
Membrane-associated fraction (MAF),<br />
determination of, 282–283<br />
Membrane effect comparison, of CPPs and other<br />
peptides, 236–238<br />
Membrane interactions, 163–183<br />
conclusions and perspectives, 180–181<br />
internalization, 177–180<br />
vesicular, 177<br />
via receptor, 177–179<br />
origin of toxicity, 179–180<br />
principles and background, 164–165<br />
structural determinations, 165–177<br />
analytical methods: conformational<br />
identifications, 166–168<br />
circular dichroism, 167<br />
diffraction, 168<br />
Fourier transform infrared<br />
spectroscopy, 167–168<br />
NMR, 166–167, 232–233<br />
bilayers, 169<br />
fluorescence, 169–177<br />
electron paramagnetic resonance (EPR)<br />
spectroscopy, 177<br />
multidisciplinary monolayer-based<br />
approach, 177–177<br />
phospholipid interactions, 168–169<br />
lipid-containing air–water interface,<br />
169<br />
lipid-free air–water interface, 168<br />
monolayer approach, 168<br />
unfolding for conjugate CPP–protein, 179<br />
Membrane-mimetic solvents, 228–229, 233–236<br />
Membrane proteins, structure prediction modeling,<br />
204–206<br />
Membrane targeting and transport (MTT) system,<br />
301–302<br />
Membrane translocating sequence (MTS) peptides,<br />
115–140<br />
arginine–proline-rich translocating peptides,<br />
129–130<br />
attaching cargo and targeting domains,<br />
124–127<br />
cationic translocating peptides, 127–129<br />
commonly used, 127<br />
future perspectives, 130–132<br />
h-region signal sequence and, 117–122<br />
applications of SN50 peptide, 119<br />
development of SN50 peptide, 117–119<br />
in integrin β 3, 122<br />
kFGF and translocation of other cargoes,<br />
119–122<br />
mechanism of membrane translocation,<br />
122–124<br />
in nucleic acid delivery, 354–356<br />
proline-rich peptides as translocating, 130<br />
signal hypothesis, 116–117<br />
Micelles, 228–229, 234–235<br />
positioning, 234–235<br />
structure induction, 234<br />
Microbial membrane-permeating peptides,<br />
377–396<br />
applications, 388–392<br />
as anti-infective agents, 388–389<br />
as delivery vehicle, 389–392<br />
experimental methods, 385–388<br />
antimicrobial activity assays, 385–386<br />
cell uptake assays, 386–388<br />
cell permeabilization assays, 386–388<br />
fluorescence microscopy and FACS,<br />
386<br />
mechanisms of action, 382–385<br />
cell-killing, 383–385<br />
cell type-specific activities, 385<br />
dual peptide activities, 384–385<br />
intracellular target inhibition, 384<br />
membrane leakage, 383–384<br />
cell uptake, 382–383<br />
cell permeation by cationic peptides,<br />
382–383<br />
receptor-mediated peptide transport<br />
and endocytosis, 383<br />
principles and background, 378–382<br />
composition and structure, 380–382<br />
origins and discovery, 380<br />
Microdilution assay, 385–386<br />
Microscopy<br />
confocal laser scanning (CLSM), 281<br />
fluorescence, 267–269, 386, see also<br />
Fluorescence studies<br />
Model amphipathic peptides (MAPs), 71–92, see<br />
also MAPs<br />
Modeling, structure prediction, 187–222<br />
conclusions, 215–218<br />
methods, 190–202<br />
atomic surface hydrophobicity (first<br />
restraint), 191–193<br />
charge simulation (third restraint), 194–197<br />
description of water–bilayer interface,<br />
190–191<br />
lipid perturbation (second restraint),<br />
193–194<br />
molecular hydrophobicity potential<br />
(MHP), 199–202<br />
Monte Carlo procedure, 198<br />
Pex2Dstat files, 198–199<br />
procedure, 197–198