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Protein Engineering, Vol. 14, No. 3, 157-160, March 2001
© 2001 Oxford University Press

Characterization of the amino acids essential for the photo- and radioprotective effects of a Bowman–Birk protease inhibitor-derived nonapeptide

Klaus H. Dittmann,1, Nuri Gueven, Claus Mayer and Hans-Peter Rodemann,1

Section of Radiobiology and Molecular Environmental Research, Department of Radiotherapy, Eberhard-Karls-University,72076 Tübingen, Germany

The Bowman–Birk protease inhibitor has been reported to exert photo- and radioprotective activity. This effect was assigned to a cyclic nonapeptide sequence which is known to contain the amino acids responsible for the anti-chymotryptic activity of the BBI. The present study indicated that linearization of the nonapeptide resulted in a significant loss of anti-proteolytic activity, whereas the photo- and radioprotective capacity persisted. Substitution of the amino acids Leu or Ser of the nonapeptide, essential for the anti-proteolytic activity, with different amino acids, indicated that rather the hydrophobic features of the amino acids in this position than charge are critical to retain the photo- and radioprotective effect. These results suggest the existence of a bifunctional peptide sequence with anti-proteolytic and photo-/radioprotective capacity. However, the lack of correlation between the photo-/radioprotective activity and the anti-proteolytic activity within the peptides generated by modification of the linear nonapeptide argues for the existence of two closely colocalized domains within the nonapeptide responsible for photo-/radioprotection and protease inhibition.


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