Structure-activity relationships of aminoglycoside-arginine conjugates that bind HIV-1 RNAs as determined by fluorescence and NMR spectroscopy.

Abstract:

:We present here a new set of aminoglycoside-arginine conjugates (AACs) that are either site-specific or per-arginine conjugates of paromomycin, neamine, and neomycin B as well as their structure-activity relationships. Their binding constants (KD) for TAR and RRE RNAs, measured by fluorescence anisotropy, revealed dependence on the number and location of arginines in the different aminoglycoside conjugates. The binding affinity of the per-arginine aminoglycosides to TAR is higher than to RRE, and hexa-arginine neomycin B is the most potent binder (KD=5 and 23 nM, respectively). The 2D TOCSY NMR spectrum of the TAR monoarginine-neomycin complex reveals binding at the bulge region of TAR.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Lapidot A,Vijayabaskar V,Litovchick A,Yu J,James TL

doi

10.1016/j.febslet.2004.10.038

keywords:

subject

Has Abstract

pub_date

2004-11-19 00:00:00

pages

415-21

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014579304012761

journal_volume

577

pub_type

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