Abstract:
:4',6-diamidino-2-phenylindole (DAPI), netropsin, and pentamidine are minor groove binders that have terminal -C(NH2)2+ groups. The hydration changes that accompany their binding to the minor groove of the (AATT)2 sequence have been studied using the osmotic stress technique with fluorescence spectroscopy. The affinity of DAPI for the binding site decreases with the increasing osmolality of the solution, resulting in acquisition of 35+/-1 waters upon binding. A competition fluorescence assay was utilized to measure the binding constants and hydration changes of the other two ligands, using the DNA-DAPI complex as the fluorescence reporter. Upon their association to the (AATT)2 binding site, netropsin and pentamidine acquire 26+/-3 and 34+/-2 additional waters of hydration, respectively. The hydration changes are discussed in the context of the terminal functional groups of the ligands and conformational changes in the DNA.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Degtyareva NN,Wallace BD,Bryant AR,Loo KM,Petty JTdoi
10.1529/biophysj.106.097451subject
Has Abstractpub_date
2007-02-01 00:00:00pages
959-65issue
3eissn
0006-3495issn
1542-0086pii
biophysj.106.097451journal_volume
92pub_type
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