Conformational study of the antitumor protein alpha-sarcin.

The antitumor protein alpha-sarcin is a single polypeptide chain produced by the mold Aspergillus giganteus. It inhibits protein synthesis in some tumor cells by inactivating the larger ribosomal subunit. The secondary structure of the molecule has been studied by circular dichroism and predictive methods. The protein contains about 40% of periodic structures, mainly located at both extremes of the polypeptide chain. beta-Turns and aperiodic conformation appear at the central part of the molecule. Two different tyrosine populations have been observed in alpha-sarcin. Attempts to correlate solvent accessibility and particular protein regions have been carried out by using CD in the near-ultraviolet region, fluorescence and absorbance spectroscopies as well as acrylamide quenching and hydropathy profiles. Five different pH-induced conformational transitions are detected. Two of them, at pH 2.5 and 10.2, are denaturing transitions. These results are explained in terms of the structural features of this molecule, and related to its ribonucleolytic activity and ability to cross cell membranes.