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CPP: Fachverband Chemische Physik und Polymerphysik

CPP 34: P6: Biomaterials and Biopolymers

CPP 34.4: Poster

Dienstag, 17. März 2015, 14:00–16:00, Poster C

Synchrotron Radiation- based FIR/THz spectroscopy for studying Membrane-targeting interactions of antimicrobial peptides — •Andrea Hornemann¹, Arne Hoehl¹, Michael Andersch^1,2, Peggy Emmer¹, Michael Vollmer², Gerhard Ulm¹, and Burkhard Beckhoff¹ — ¹Physikalisch-Technische Bundesanstalt, Berlin, Germany — ²University of Applied Sciences in Brandenburg, Brandenburg, Germany

The development of new infrared radiation sources has initiated opportunities for exploring the molecular structure of many (bio-) materials in the far-infrared/terahertz spectral region. The identification of thin organic films derived from peptide layers at polymer/organic interfaces was performed by Synchrotron Radiation (SR-) based FTIR spectroscopy at PTB’s Metrology Light Source. For bioanalytical applications, the FIR/THz spectroscopic technique offers a unique tool for a distinct identification of biochemical components by their vibrational spectra. Peptide films were studied in the spectral region from 400 cm^-1 to 5 cm^-1. This spectral region complements the mid-infrared spectral range where molecules such as proteins deliver characteristic modes, and entails additional molecular information on torsion and bending modes of the carbon backbone and H-bonds of biomolecules. We discuss the signatures of different membrane-targeting antimicrobial peptides that display defined secondary-structure motifs. Our approach entails T-dependent studies between between 298 K and 10 K.