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Studies on anticancer activities of antimicrobial peptides.
TLDR
Various studies on different cationic antimicrobial peptides that exhibit cytotoxic activity against cancer cells are reviewed and the suitability of cancer cell-targeting AMPs as cancer therapeutics is discussed. Expand
LL-37, the only human member of the cathelicidin family of antimicrobial peptides.
TLDR
LL-37, the only cathelicidin-derived antimicrobial peptide found in humans, is shown to exhibit a broad spectrum of antimicrobial activity and has been found to have additional defensive roles such as regulating the inflammatory response and chemo-attracting cells of the adaptive immune system to wound or infection sites. Expand
Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37.
TLDR
A toroidal pore mechanism of lipid bilayer disruption by LL-37 is supported, and it is shown that micelles or other small, rapidly tumbling membrane fragments are not formed in the presence of the peptide, excluding a detergent-like mechanism. Expand
Ultrastrong and Stiff Layered Polymer Nanocomposites
TLDR
A high level of ordering of the nanoscale building blocks, combined with dense covalent and hydrogen bonding and stiffening of the polymer chains, leads to highly effective load transfer between nanosheets and the polymer. Expand
Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment.
TLDR
The structure of the naturally occurring peptide in detergent micelles at a neutral pH has an overall kinked helix motif, with residues 7-17 and 21-28 in a helical conformation, and with a 3(10) helix from Gly 33-Asn 35. Expand
MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain.
TLDR
This work shows that MSI-78 induces significant changes in lipid bilayers via positive curvature strain and presents a model consistent with both the observed spectral changes and previously published work. Expand
NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles.
TLDR
Results support the proposed nonpore carpet-like mechanism of action, in agreement with the solid-state NMR studies, and pave the way for understanding the function of the mature LL-37 at the atomic level. Expand
Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37.
TLDR
Differential scanning calorimetry and deuterium ((2)H) NMR experiments on acyl chain perdeuterated lipids demonstrate that LL-37 inserts into the hydrophobic region of the bilayer and alters the chain packing and cooperativity, and shows that hydrophobia interactions between LL- 37 and the Hydrophobic acyl chains are as important for the ability of this peptide to disrupt lipid bilayers as its electrostatic interactions with the polar headgroups. Expand
Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin.
TLDR
The mechanism of membrane interaction of two amphipathic antimicrobial peptides, MSI-78 and MSI-594, derived from magainin-2 and melittin, is presented and 2H-NMR experiments with selectively deuterated lipids reveal peptide-induced disorder in the methylene units of the lipid acyl chains. Expand
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