Fluorescence spectroscopy and molecular dynamics simulations in studies on the mechanism of membrane destabilization by antimicrobial peptides |
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Authors: | Gianfranco Bocchinfuso Sara Bobone Claudia Mazzuca Antonio Palleschi Lorenzo Stella |
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Institution: | 1.Dipartimento di Scienze e Tecnologie Chimiche,Università di Roma Tor Vergata,Rome,Italy;2.IRCCS Neuromed,Pozzilli,Italy |
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Abstract: | Since their initial discovery, 30 years ago, antimicrobial peptides (AMPs) have been intensely investigated as a possible
solution to the increasing problem of drug-resistant bacteria. The interaction of antimicrobial peptides with the cellular
membrane of bacteria is the key step of their mechanism of action. Fluorescence spectroscopy can provide several structural
details on peptide–membrane systems, such as partition free energy, aggregation state, peptide position and orientation in
the bilayer, and the effects of the peptides on the membrane order. However, these “low-resolution” structural data are hardly
sufficient to define the structural requirements for the pore formation process. Molecular dynamics simulations, on the other
hand, provide atomic-level information on the structure and dynamics of the peptide–membrane system, but they need to be validated
experimentally. In this review we summarize the information that can be obtained by both approaches, highlighting their versatility
and complementarity, suggesting that their synergistic application could lead to a new level of insight into the mechanism
of membrane destabilization by AMPs. |
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Keywords: | |
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