It has recently been shown that Fe(I) complexes of ADP or ATP generate OH radicals with H2O2 in a Fenton-type reaction. The OH radicals can be detected by using 5,5-dimethyl-1-pyrroline-N-oxide (DMPO) as a spin trap in electron spin resonance spectroscopy. All the biologically occurring amino acids, some related compounds and several proteins (histone, bovine serum albumin, collagen) were tested as OH radical scavengers against DMPO. The tested compounds competed with DMPO in trapping OH radicals to various extents as shown by the decrease of signal intensity of DMPO-OH spin-adduct. The tested compounds did not oxidize Fe(II) itself, with the only exception being tyrosine, as revealed by properly designed ferrozine reaction. Some of the amino acids reacted also with the DMPO-OH spin-adduct to a certain extent, whereas others did not. The formation of carbon centered organic radicals of the amino acids could be detected under the influence of OH radicals by using the spin traps phenyl-tert-butylnitrone (PBN) and alpha-pyridyl-1-oxide-N-tert-butylnitrone (4-POBN). The proteins, however, did not react with these spin traps. One can conclude that the amino acids and proteins can be targets of OH radical damage even in vivo, and such phenomena may be of importance in the deterioration of the conformation of proteins, e.g., during aging or in some pathological processes.