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Investigating Membrane-Mediated Antimicrobial Peptide Interactions with Synchrotron Radiation Far-Infrared Spectroscopy

  • 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, providesSynchrotron 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.zeige mehrzeige weniger

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Metadaten
Verfasserangaben:Andrea HornemannORCiD, Diane Madeleine EichertORCiD, Arne HoehlORCiD, Brigitte TierschORCiD, Gerhard Ulm, Maxim G. RyadnovORCiDGND, Burkhard Beckhoff
DOI:https://doi.org/10.1002/cphc.202100815
ISSN:1439-4235
ISSN:1439-7641
Pubmed ID:https://pubmed.ncbi.nlm.nih.gov/35032089
Titel des übergeordneten Werks (Englisch):ChemPhysChem : a European journal of chemical physics and physical chemistry
Verlag:Wiley-VCH
Verlagsort:Weinheim
Publikationstyp:Wissenschaftlicher Artikel
Sprache:Englisch
Datum der Erstveröffentlichung:14.01.2022
Erscheinungsjahr:2022
Datum der Freischaltung:06.03.2024
Freies Schlagwort / Tag:IR spectroscopy; antimicrobial peptides; electrostatic interactions; phospholipid membranes; protein folding
Band:23
Ausgabe:4
Aufsatznummer:e202100815
Seitenanzahl:11
Fördernde Institution:EURAMET; European Community's Seventh Framework Programme, ERA-NET Plus; [217257]; Projekt DEAL
Organisationseinheiten:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Physik und Astronomie
DDC-Klassifikation:5 Naturwissenschaften und Mathematik / 53 Physik / 530 Physik
Peer Review:Referiert
Publikationsweg:Open Access / Hybrid Open-Access
Lizenz (Deutsch):License LogoCC-BY - Namensnennung 4.0 International
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