Datta, G and Hosur, RV and Verma, NC and Khetrapal, CL and Gurnani, S (1989) Mechanism of interaction of the antileukemic drug cytosine arabinoside with aromatic peptides : role of sugar conformation and peptide backbone. In: Physiological Chemistry & Physics & Medical NMR, 21 (4). 279-288 .Full text not available from this repository.
Interaction of the antileukemic drugs, cytosine-arabinoside (Ara-C) and adenosine-arabinoside (Ara-A) and a structural analogue, cytidine, with aromatic dipeptides has been studied by fluorescence and NMR spectroscopy. Ara-C and cytidine bind tryptophanyl and histidyl dipeptides but not tyrosyl dipeptides, while Ara-A does not bind to any of them. Both studies indicate association involving stacking of aromatic moieties. NMR spectra also indicate a protonation of the histidine moiety by Ara-C. In case of cytidine, the chemical shifts observed on binding to His-Phe imply that the backbone protons of the dipeptide participate in the binding. The conformation of the sugar and the base seem to play a very important role in the binding phenomenon as three similar molecules, Ara-C, Ara-A and cytidine bind in totally different ways.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Pacific Press Inc., New York.|
|Department/Centre:||Division of Chemical Sciences > Sophisticated Instruments Facility|
|Date Deposited:||19 Oct 2010 07:19|
|Last Modified:||19 Oct 2010 07:19|
Actions (login required)