Investigating Membrane‐Mediated Antimicrobial Peptide Interactions with Synchrotron Radiation Far‐Infrared Spectroscopy. Issue 4 (14th January 2022)
- Record Type:
- Journal Article
- Title:
- Investigating Membrane‐Mediated Antimicrobial Peptide Interactions with Synchrotron Radiation Far‐Infrared Spectroscopy. Issue 4 (14th January 2022)
- Main Title:
- Investigating Membrane‐Mediated Antimicrobial Peptide Interactions with Synchrotron Radiation Far‐Infrared Spectroscopy
- Authors:
- Hornemann, Andrea
Eichert, Diane M.
Hoehl, Arne
Tiersch, Brigitte
Ulm, Gerhard
Ryadnov, Maxim G.
Beckhoff, Burkhard - Abstract:
- Abstract: 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. Abstract : Synchrotron radiation far‐infrared spectroscopy enables studying the mechanistic behaviour of antimicrobial peptides in reconstituted membranes, and monitoring membrane‐mediated antimicrobial interactions. Membrane polarity, antimicrobialAbstract: 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. Abstract : Synchrotron radiation far‐infrared spectroscopy enables studying the mechanistic behaviour of antimicrobial peptides in reconstituted membranes, and monitoring membrane‐mediated antimicrobial interactions. Membrane polarity, antimicrobial peptide membrane‐mediated conformation, and related electrostatic interactions are key aspects leading to membrane destabilisation. … (more)
- Is Part Of:
- Chemphyschem. Volume 23:Issue 4(2022)
- Journal:
- Chemphyschem
- Issue:
- Volume 23:Issue 4(2022)
- Issue Display:
- Volume 23, Issue 4 (2022)
- Year:
- 2022
- Volume:
- 23
- Issue:
- 4
- Issue Sort Value:
- 2022-0023-0004-0000
- Page Start:
- n/a
- Page End:
- n/a
- Publication Date:
- 2022-01-14
- Subjects:
- antimicrobial peptides -- electrostatic interactions -- IR spectroscopy -- phospholipid membranes -- protein folding
Chemistry, Physical and theoretical -- Periodicals
541.05 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1439-7641 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/cphc.202100815 ↗
- Languages:
- English
- ISSNs:
- 1439-4235
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3172.310500
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 21117.xml