Journal Article

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

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

in Protein Engineering, Design and Selection

Volume 14, issue 3, pages 157-160
Published in print March 2001 | ISSN: 1741-0126
Published online March 2001 | e-ISSN: 1741-0134 | DOI: https://dx.doi.org/10.1093/protein/14.3.157
Characterization of the amino acids essential for the photo- and radioprotective effects of a Bowman–Birk protease inhibitor-derived nonapeptide

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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.

Keywords: BBI-derived peptide; clonogenic survival; photoprotection; protease inhibitor; radioprotection

Journal Article.  3474 words.  Illustrated.

Subjects: Proteins

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