文摘
The exceptionally high affinity of biotin toward avidin and streptavidin is at the basis of (strept)avidin-biotinbiotechnology, which has numerous applications in life sciences. Recent biotin developments for in vivo and invitro acylation of selective targeted protein and intein-mediated site specific protein biotinylation require the freebiotin carboxyl function to covalently bind with the targeted protein. However, recently this carboxylic functionhas been used to substitute biotin with numerous ligands and flags. In the present work, we propose the N-1'labeling possibilities of biotin, keeping the valeric chain free. We describe liquid and solid-phase syntheses offunctionalized biotin N-1' derivatives. Although the N-1' modification involves a two-log decrease in affinity, invitro these molecules kept their high avidin affinity (around 10-12 M) and the in vivo acylation ability of newbiotin derivatives.