The radiolysis and radioracemization of poly-L-leucines

Abstract

The brief history of the discovery of radioracemization, the racemization of an optically active substance induced by ionizing radiation, is reviewed. Our early studies involving the radiolysis and radioracemization of D- and L-leucine using gamma radiation from a 111-TBq 60Co gamma-ray source are described briefly, as are later experiments involving other protein amino acids and their salts, as well as the nonprotein amino acid, isovaline. The implications of the results of such studies for the Vester-Ulbricht mechanism which proposes longitudinally polarized beta radiation as the origin of molecular chirality, for the cosmological question of the enantiomeric compositions of amino acids in the Murchison meteorite, and for the use of D/L ratios of amino acids for geochronological and geothermal estimates are reviewed briefly. These past radiolysis-radio- racemization studies have involved only monomeric amino acids. The present research, extending such investigations to two homochiral L-leucine polypeptides, (L-Leu)10 and (L-Leu)78, was undertaken to see if a polymer of an amino acid might be more stable to radiolysis and radioracemization than the corresponding monomer. It was found that these polypeptides were more stable to radiolysis than was the leucine monomer, but that the extents of radioracemization in all samples were comparable.