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

journal contribution
posted on 2023-05-17, 13:04 authored by Dittmann, KH, Nuri GuvenNuri Guven, Mayer, C, Rodemann, HP
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.

History

Publication title

Protein Engineering

Volume

14

Pagination

157-160

ISSN

0269-2139

Department/School

School of Pharmacy and Pharmacology

Publisher

Oxford Univ Press

Place of publication

Great Clarendon St, Oxford, England, Ox2 6Dp

Rights statement

Copyright 2001 Oxford University Press

Repository Status

  • Restricted

Socio-economic Objectives

Expanding knowledge in the biological sciences

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