CONICET | Buscador de Institutos y Recursos Humanos

The structure of peptide fragments was studied using action IR spectroscopy. We report on room temperature IR spectra of b4 fragments of protonated GGGGG, AAAAA, and YGGFL in the X-H (X=C, N, O) stretching region. Experiments were performed with a Tandem mass spectrometer combined with table top tunable laser, and the multiple photon absorption process was assisted using an auxiliary high power CO2 laser. These experiments provided well-resolved spectra with relatively narrow peaks in the X-H (X=C, N, O) stretching region for the b4 fragments of protonated GGGGG, AAAAA, and YGGFL. The 3200-3700 cm-1rangeof the first two of these spectra are rather similar, and the corresponding peaks can be assigned based on the classical b ion structure that has a linear backbone terminated by the oxazolone ring at the C-terminus and ionizing proton residing on the oxazolone ring nitrogen. The spectrum of the b4 of YGGFL, on the other hand, is different from the two others, and is characterized by a band observed near 3238 cm-1. Similar band positions have recently been reported for one of the four isomers of the b4 of YGGFL studied using double resonance IR/UV technique. As proposed in this study, the IR spectrum of this ion at room temperature can also be assigned to a linear N-terminal amine protonated oxazolone structure. However, an alternative assignment could be proposed since our room temperature IR spectrum of the b4 of YGGFL nicely matches with the predicted IR absorption spectrum of a macrocyclic structure. Since not all experimental IR features are unambiguously assigned based on the available literature structures, further theoretical studies will be required to fully exploit the benefits offered by IR spectroscopy in the X-H (X=C, N, O) stretching region.