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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, HPThe 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 EngineeringVolume
14Pagination
157-160ISSN
0269-2139Department/School
School of Pharmacy and PharmacologyPublisher
Oxford Univ PressPlace of publication
Great Clarendon St, Oxford, England, Ox2 6DpRights statement
Copyright 2001 Oxford University PressRepository Status
- Restricted