Impacts of solvation on photo-damage of polypeptides: Modulation and biological implications

We investigate the photon/matter interactions between soft X-rays and three selected polypeptides, poly-glycine (poly-Gly), poly-L-arginine (poly-Arg), and poly-l-lysine (poly-Lys), where the effects of molecular packing under the influence of solvent, e.g., water, substrates (Au foil or Si wafer) and X-ray irradiation under different durations were systematically investigated. Compared with negligible photo-damage on bare polypeptide powders, significantly enhanced degradation in pre-solvated polypeptides was observed likely because of the formation photo-generated radicals. X-ray photoemission spectroscopy (XPS) were employed as the analysis means to identify and quantify the chemical changes, especially the high-resolution photoemission spectra of C 1s, O 1s, N 1s and their evolution under continuous X-ray irradiation. The photo-degradation was found to preferentially occur on the CO entity in poly-Gly and the guanidinium group in poly-Arg. In poly-Arg, deprotonation occurs via the switch from zwittterionic to a neutral configuration, whereas poly-Lys deprotonates by directly losing the corresponding amine. The critical role of the interactions between amino acids, the building blocks of protein and almost all forms of biological activities, and the free-radical-generating living environment under irradiation was critically analyzed. The present study found that the preparation history of a sample, especially its inadvertent exposure to the sources of H₂O, O₂ and OH, could significantly alter the outcome of a radiation-related chemical process. Implications on the non-destructive probe of biologically important systems using physical methods involving X-rays were discussed as well.