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Abstract
The Bowman-Birk protease inhibitor (BBI), a serine-protease inhibitor, has been reported
to exert both anticarcinogenic and radioprotective activity. In this work we examined
whether this effect is mediated through inhibition of serine-proteases of the trypsin-chymotrypsin
type. Using linearized forms of BBI, evidence will be provided that the secondary
structure, obligatory for the protease inhibitory function, is not necessary for the
radioprotective effect. Detailed analysis indicated that the radioprotective effect
is correlated with the chymotrypsin-inhibitory region of the molecule. Using a synthetic
nonapeptide lacking protease inhibitor activity, the radioprotective effect of the
total BBI molecule could be mimicked, indicating that the radioprotective effect is
independent of the protease inhibitor function.