Probing the formation of isolated cyclo-FF peptide clusters by far-infrared action spectroscopy.
Autor: | Bakels S; Radboud University, FELIX Laboratory, Institute for Molecules and Materials, Toernooiveld 7, 6525 ED Nijmegen, The Netherlands., Stroganova I; Division of BioAnalytical Chemistry, AIMMS Amsterdam Institute of Molecular and Life Sciences, Vrije Universiteit Amsterdam, De Boelelaan 1108, 1081 HV, Amsterdam, The Netherlands. a.m.rijs@vu.nl.; Radboud University, FELIX Laboratory, Institute for Molecules and Materials, Toernooiveld 7, 6525 ED Nijmegen, The Netherlands., Rijs AM; Division of BioAnalytical Chemistry, AIMMS Amsterdam Institute of Molecular and Life Sciences, Vrije Universiteit Amsterdam, De Boelelaan 1108, 1081 HV, Amsterdam, The Netherlands. a.m.rijs@vu.nl. |
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Jazyk: | angličtina |
Zdroj: | Physical chemistry chemical physics : PCCP [Phys Chem Chem Phys] 2021 Sep 29; Vol. 23 (37), pp. 20945-20956. Date of Electronic Publication: 2021 Sep 29. |
DOI: | 10.1039/d1cp03237b |
Abstrakt: | Small cyclic peptides containing phenylalanine residues are prone to aggregate in the gas phase into highly hydrophobic chains. A combination of laser desorption, mass spectrometry and conformational selective IR-UV action spectroscopy allows us to obtain detailed structural insights into the formation processes of the cyclic L-phenylalanyl-L-phenylalanine dipeptide (named cyclo-FF) aggregates. The rigid properties of cyclo-FF result in highly resolved IR spectra for the smaller clusters ( n ≤ 3) and corresponding conformational assignments. For the higher order clusters ( n > 3) the spectra are less resolved, however the observed ratios, peak positions and trends in IR shifts are key to make predictions on their structural details. Whereas the mid-IR spectral region between 1000-1800 cm -1 turns out to be undiagnostic for these small aggregates and the 3 μm region only for specific calculated structures, the far-IR contains valuable information that allows for clear assignments. |
Databáze: | MEDLINE |
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