Stability of non-proteinogenic amino acids to UV and gamma irradiation

Almost all living organisms on Earth utilize the same 20 amino acids to build their millions of different proteins, even though there are hundreds of amino acids naturally occurring on Earth. Although it is likely that both the prebiotic and the current environment of Earth shaped the selection of these 20 proteinogenic amino acids, environmental conditions on extraterrestrial planets and moons are known to be quite different than those on Earth. In particular, the surfaces of planets and moons such as Mars, Europa and Enceladus have a much greater flux of UV and gamma radiation impacting their surface than that of Earth. Thus, if life were to have evolved extraterrestrially, a different lexicon of amino acids may have been selected due to different environmental pressures, such as higher radiation exposure. One fundamental property an amino acid must have in order to be of use to the evolution of life is relative stability. Therefore, we studied the stability of three different proteinogenic amino acids (tyrosine, phenylalanine and tryptophan) as compared with 20 non-proteinogenic amino acids that were structurally similar to the aromatic proteinogenic amino acids, following ultraviolet (UV) light (254, 302, or 365 nm) and gamma-ray irradiation. The degree of degradation of the amino acids was quantified using an ultra-high performance liquid chromatography-mass spectrometer (UPLC-MS). The result showed that many non-proteinogenic amino acids had either equal or increased stability to certain radiation wavelengths as compared with their proteinogenic counterparts, with fluorinated phenylalanine and tryptophan derivatives, in particular, exhibiting enhanced stability as compared with proteinogenic phenylalanine and tryptophan amino acids following gamma and select UV irradiation