• search hit 3 of 10
Back to Result List

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.show moreshow less

Export metadata

Additional Services

Search Google Scholar Statistics
Metadaten
Author details: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
Title of parent work (English):ChemPhysChem : a European journal of chemical physics and physical chemistry
Publisher:Wiley-VCH
Place of publishing:Weinheim
Publication type:Article
Language:English
Date of first publication:2022/01/14
Publication year:2022
Release date:2024/03/06
Tag:IR spectroscopy; antimicrobial peptides; electrostatic interactions; phospholipid membranes; protein folding
Volume:23
Issue:4
Article number:e202100815
Number of pages:11
Funding institution:EURAMET; European Community's Seventh Framework Programme, ERA-NET Plus; [217257]; Projekt DEAL
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Physik und Astronomie
DDC classification:5 Naturwissenschaften und Mathematik / 53 Physik / 530 Physik
Peer review:Referiert
Publishing method:Open Access / Hybrid Open-Access
License (German):License LogoCC-BY - Namensnennung 4.0 International
Accept ✔
This website uses technically necessary session cookies. By continuing to use the website, you agree to this. You can find our privacy policy here.