@article {2117,
	title = {Lipid-specific binding of the calcium-dependent antibiotic daptomycin leads to changes in lipid polymorphism of model membranes},
	journal = {Chemistry and Physics of Lipids},
	volume = {154},
	number = {2},
	year = {2008},
	note = {ISI Document Delivery No.: 336MXTimes Cited: 8Cited Reference Count: 41Jung, David Powers, Jon Paul Straus, Suzana K. Hancock, Robert E. W.},
	month = {Aug},
	pages = {120-128},
	type = {Article},
	abstract = {Daptomycin is a cyclic anionic lipopeptide with an antibiotic activity that is completely dependent on the presence of calcium (as Ca2+). In a previous study [Jung et al., 2004. Chem. Biol. 11, 949-957], it was concluded that daptomycin underwent two Ca2+-dependent structural transitions, whereby the first transition was solely dependent on Ca2+, while the second transition was dependent on both Ca2+ and the presence of negatively charged lipids that allowed daptomycin to insert into and perturb bilayer membranes with acidic character. Differences in the interaction of daptomycin with acidic and neutral membranes were further investigated by spectroscopic means. The lack of quenching of intrinsic fluorescence by the water-soluble quencher, KI, confirmed the insertion of the daptomycin Trp residue into the membrane bilayer, while the kynurenine residue was inaccessible even in an aqueous environment. Differential scanning calorimetry (DSC) indicated that the binding of daptomycin to neutral bilayers occurred through a combination of electrostatic and hydrophobic interactions, while the binding of daptomycin to Mayers containing acidic lipids primarily involved electrostatic interactions. The binding of daptomycin to acidic membranes led to the induction of non-lamellar lipid phases and membrane fusion. (C) 2008 Elsevier Ireland Ltd. All rights reserved.},
	keywords = {ANTIMICROBIAL PEPTIDES, Daptomycin, DSC, FLUORESCENCE, lipopeptide, LY146032, membrane fusion, MIMETIC SYSTEMS, MODEL MEMBRANES, P-31 NMR, PHASE-TRANSITIONS, PHOSPHOLIPIDS, RESONANCE ENERGY-TRANSFER, STAPHYLOCOCCUS-AUREUS, X-RAY-DIFFRACTION},
	isbn = {0009-3084},
	url = {<Go to ISI>://000258369200006},
	author = {Jung, D. and Powers, J. P. and Straus, S. K. and Hancock, R. E. W.}
}
@article {1291,
	title = {Plasticity of influenza haemagglutinin fusion peptides and their interaction with lipid bilayers},
	journal = {Biophysical Journal},
	volume = {88},
	number = {1},
	year = {2005},
	note = {ISI Document Delivery No.: 884MYTimes Cited: 36Cited Reference Count: 72},
	month = {Jan},
	pages = {25-36},
	type = {Article},
	abstract = {A detailed molecular dynamics study of the haemagglutinin fusion peptide (N-terminal 20 residues of the HA2 subunits) in a model bilayer has yielded useful information about the molecular interactions leading to insertion into the lipids. Simulations were performed on the native sequence, as well as a number of mutant sequences, which are either fusogenic or nonfusogenic. For the native sequence and fusogenic mutants, the N-terminal 11 residues of the fusion peptides are helical and insert with a tilt angle of similar to30degrees with respect to the membrane normal, in very good agreement with experimental data. The tilted insertion of the native sequence peptide leads to membrane bilayer thinning and the calculated order parameters show larger disorder of the alkyl chains. These results indicate that the lipid packing is perturbed by the fusion peptide and could be used to explain membrane fusion. For the nonfusogenic sequences investigated, it was found that most of them equilibrate parallel to the interface plane and do not adopt a tilted conformation. The presence of a charged residue at the beginning of the sequence (G1E mutant) resulted in a more difficult case, and the outcomes do not fall straightforwardly into the general picture. Sequence searches have revealed similarities of the fusion peptide of influenza haemagglutinin with peptide sequences such as segments of porin, amyloid ab peptide, and a peptide from the prion sequence. These results confirm that the sequence can adopt different folds in different environments. The plasticity and the conformational dependence on the local environment could be used to better understand the function of fusion peptides.},
	keywords = {ANALOGS, CONFORMATION, HEMAGGLUTININ, MEDIATED MEMBRANE-FUSION, MODEL MEMBRANES, MOLECULAR-DYNAMICS SIMULATION, MULTIPLE ALIGNMENT, RECEPTOR-BINDING, SEQUENCE, VIRAL FUSION, VIRUS},
	isbn = {0006-3495},
	url = {<Go to ISI>://000226090900006},
	author = {Vaccaro, L. and Cross, K. J. and Kleinjung, J. and Straus, S. K. and Thomas, D. J. and Wharton, S. A. and Skehel, J. J. and Fraternali, F.}
}
