Introduction: The majority of attempts to stop smoking end in failure. One way to improve success may be to explore different combinations of existing cessation medications.

Aims: This observational study examined ‘triple therapy’ (varenicline + nicotine patch + nicotine lozenge) in 36 smokers trying to quit.

Methods: A 12-week, observational study exploring tolerability, via adverse events (AEs) elicited at each of nine phone assessments. Secondary outcomes included satisfaction rates, medication changes and self-reported quit rates at week 12.

Results: Thirty five of thirty six participants reported at least one AE. Insomnia (75%), abnormal dreams (72%) and nausea (64%) were most common. Most were mild to moderate. No deaths, hospitalisations, cardiovascular events or suicidality were reported. Six participants (17%) decreased the dose of at least one medication, 5 (14%) decreased the dose then discontinued at least one medication and 13 (36%) discontinued at least one medication without trying a lesser dose. Participants were highly satisfied with their medications, and 58% reported quitting at 12 weeks, with 38% reporting prolonged abstinence.

Conclusions: Despite high rates of AEs and medication changes, high rates of satisfaction and self-reported quitting, with no serious AEs, were observed with triple therapy. Additional data on tolerability and efficacy are needed.

Trial Registration:Clinicaltrials.gov number NCT02681510.

Extended abstract of a paper presented at Microscopy and Microanalysis 2004 in Savannah, Georgia, USA, August 1–5, 2004.

Dihydrohpoamide acetyl transferase (E2), a catalytic and structural component of a multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate, forms the central core to which the other components are bound. We have utilized protein engineering and 3-D electron microscopy to study the structural organization of the largest multienzyme complex known (Mr ∼ 107). The structures of the truncated 60-mer core (tE2) and complexes of the tE2 associated with a binding protein (BP), and the BP associated with its dihydrohpoamide dehydrogenase (BP'E3) and the intact E2 associated with BP and the pyruvate dehydrogenase (E1) were determined (Figs. 1 and 2). The tE2 core is a pentagonal dodecahedron consisting of 20 cone-shaped trimers interconnected by 30 bridges.

Previous studies have given rise to the generally accepted belief that BP and BP'E3 components are bound on the outside of the E2 scaffold and that E1 is similarly bound to the core in variable positions by flexible tethers.