TY  - JOUR
A1  - Hornemann, Andrea
A1  - Eichert, Diane Madeleine
A1  - Hoehl, Arne
A1  - Tiersch, Brigitte
A1  - Ulm, Gerhard
A1  - Ryadnov, Maxim G.
A1  - Beckhoff, Burkhard
T1  - Investigating Membrane-Mediated Antimicrobial Peptide Interactions with Synchrotron Radiation Far-Infrared Spectroscopy
JF  - ChemPhysChem : a European journal of chemical physics and physical chemistry
N2  - Synchrotron radiation-based Fourier transform infrared spectroscopy enables access to vibrational information from mid over far infrared to even terahertz domains. This information may prove critical for the elucidation of fundamental bio-molecular phenomena including folding-mediated innate host defence mechanisms. Antimicrobial peptides (AMPs) represent one of such phenomena. These are major effector molecules of the innate immune system, which favour attack on microbial membranes. AMPs recognise and bind to the membranes whereupon they assemble into pores or channels destabilising the membranes leading to cell death. However, specific molecular interactions responsible for antimicrobial activities have yet to be fully understood. Herein we probe such interactions by assessing molecular specific variations in the near-THz 400-40 cm(-1) range for defined helical AMP templates in reconstituted phospholipid membranes. In particular, we show that a temperature-dependent spectroscopic analysis, supported by 2D correlative tools, provides direct evidence for the membrane-induced and folding-mediated activity of AMPs. The far-FTIR study offers a direct and information-rich probe of membrane-related antimicrobial interactions.
KW  - antimicrobial peptides
KW  - electrostatic interactions
KW  - IR spectroscopy
KW  - phospholipid membranes
KW  - protein folding
Y1  - 2022
U6  - https://doi.org/10.1002/cphc.202100815
SN  - 1439-4235
SN  - 1439-7641
VL  - 23
IS  - 4
PB  - Wiley-VCH
CY  - Weinheim
ER  -