[HTML][HTML] Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic …

Y Shai - Biochimica et Biophysica Acta (BBA)-Biomembranes, 1999 - Elsevier
Permeation of the cell membrane leading to cell death is a mechanism used by a large
number of membrane-lytic peptides. Some are linear, mostly helical, and others contain one …

Mode of action of linear amphipathic α‐helical antimicrobial peptides

Z Oren, Y Shai - Peptide Science, 1998 - Wiley Online Library
The increasing resistance of bacteria to conventional antibiotics resulted in a strong effort to
develop antimicrobial compounds with new mechanisms of action. Antimicrobial peptides …

Machine learning and data science in soft materials engineering

AL Ferguson - Journal of Physics: Condensed Matter, 2017 - iopscience.iop.org
In many branches of materials science it is now routine to generate data sets of such large
size and dimensionality that conventional methods of analysis fail. Paradigms and tools from …

Action of antimicrobial peptides: two-state model

HW Huang - Biochemistry, 2000 - ACS Publications
The argument and experimental evidence are presented for a two-state model that explains
the action of both helical and β-sheet antimicrobial peptides after they bind to the plasma …

Magainins as paradigm for the mode of action of pore forming polypeptides

K Matsuzaki - Biochimica et Biophysica Acta (BBA)-Reviews on …, 1998 - Elsevier
Magainins are a class of antimicrobial peptides discovered in the skin of Xenopus laevis.
The peptides kill bacteria by permeabilizing the cell membranes without exhibiting …

[HTML][HTML] The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy

B Bechinger - Biochimica et Biophysica Acta (BBA)-Biomembranes, 1999 - Elsevier
Linear peptide antibiotics have been isolated from amphibians, insects and humans and
used as templates to design cheaper and more potent analogues for medical applications …

[HTML][HTML] Molecular mechanism of antimicrobial peptides: the origin of cooperativity

HW Huang - Biochimica et Biophysica Acta (BBA)-Biomembranes, 2006 - Elsevier
Based on very extensive studies on four peptides (alamethicin, melittin, magainin and
protegrin), we propose a mechanism to explain the cooperativity exhibited by the activities of …

Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin.

B Bechinger - 1997 - cabidigitallibrary.org
The structure and functions of membrane-active peptides are extensively reviewed. These
peptides including cecropins from insects, melittin from honey bees (Apis mellifera) and …

Structure and orientation of the antibiotic peptide magainin in membranes by solid‐state nuclear magnetic resonance spectroscopy

B Bechinger, M Zasloff, SJ Opella - Protein Science, 1993 - Wiley Online Library
Magainin 2 is a 23‐residue peptide that forms an amphipathic α‐helix in membrane
environments. It functions as an antibiotic and is known to disrupt the electrochemical …

Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes

E Gazit, IR Miller, PC Biggin, MSP Sansom… - Journal of molecular …, 1996 - Elsevier
Cecropins are positively charged antibacterial peptides that act by permeating the
membrane of susceptible bacteria. To gain insight into the mechanism of membrane …