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BACKGROUND Lone atrial fibrillation (AF) is thought to be a benign type or an early stage of the disease. OBJECTIVE This study sought to compare the left atrium (LA) substrate using delayed-enhanced magnetic resonance imaging (DE-MRI) in patients with lone AF versus those with comorbidities. METHODS Forty of 333 included patients met criteria for lone AF. All patients underwent DE-MRI to quantify atrial fibrosis as a marker for structural remodeling (SRM) and underwent catheter ablation. Based on the degree of SRM, patients were staged into 4 groups: Utah I (5% LA wall enhancement), Utah II (5% to 20%), Utah III (20% to 35%), or Utah IV (35%). RESULTS Distribution in Utah I to IV was comparable in patients with lone AF and non‐lone AF. In both groups, a number of patients showed extensive SRM. Mean enhancement (14.08 8.94 vs. 16.94 11.37) was not significantly different between the 2 groups (P .0721). In the lone AF group, catheter ablation was successful in suppressing AF in all of Utah I, 81.82% of Utah II, 62.5% of Utah III, and none of Utah IV patients. Similar results were achieved in the non‐lone AF group. Outcome after ablation was significantly dependent on the SRM of the LA (P .001). CONCLUSION The degree of LA structural remodeling as detected using DE-MRI is independent of AF type and associated comorbidities. Selecting appropriate treatment candidates based on the quality and quantity of atrial fibrosis using DE-MRI would improve procedural outcome and avoid unnecessary intervention.

We have developed a novel method to study the interactions of nucleic acids with cationic species. The method, called phosphorus relaxation enhancement (PhoRE), uses (1)H-detected (31)P NMR of exogenous probe ions to monitor changes in the equilibrium between free Mn(2+) and Mn(2+) bound to the RNA. To demonstrate the technique, we describe the interactions of four RNA molecules with metal ions (K(+) and Mg(2+)), a small molecule drug (neomycin b), and a cationic peptide (RSG1.2). In each case, cationic ligand binding caused Mn(2+) to be displaced from the RNA. Free Mn(2+) was determined from its effect on the T(2) NMR relaxation rate of either phosphite (HPO(3)(2-)) or methyl phosphite (MeOPH, CH(3)OP(H)O(2-)). Using this method, the effects of [RNA] as low as 1 microM could be measured in 20 min of accumulation using a low field (200 MHz) instrument without pulsed field gradients. Cation association behavior was sequence and [RNA] dependent. At low [K(+)], Mn(2+) association with each of the RNAs decreased with increasing [K(+)] until approximately 40 mM, where saturation was reached. While saturating K(+) displaced all the bound Mn(2+) from a 31-nucleotide poly-uridine (U(31)), Mn(2+) remained bound to each of three hairpin-forming sequences (A-site, RRE1, and RRE2), even at 150 mM K(+). Bound Mn(2+) was displaced from each of the hairpins by Mg(2+), allowing determination of Mg(2+) dissociation constants (K(d,Mg)) ranging from 50 to 500 microM, depending on the RNA sequence and [K(+)]. Both neomycin b and RSG1.2 displaced Mn(2+) upon binding the hairpins. At [RNA] approximately 3 microM, RRE1 bound a single equivalent of RSG1.2, whereas neither RRE2 nor A-site bound the peptide. These behaviors were confirmed by fluorescence polarization using TAMRA-labeled peptide. At 2.7 microM RNA, the A-site hairpin bound a single neomycin b molecule. The selectivity of RSG1.2 binding was greatly diminished at higher [RNA]. Similarly, each hairpin bound multiple equivalents of neomycin at the higher [RNA]. These results demonstrate the utility of the PhoRE method for characterizing metal binding behaviors of nucleic acids and for studying RNA/ligand interactions.