Suspected intraoperative formation of left atrial thrombus in a patient with atrial fibrillation receiving bridging anticoagulation therapy.

We present a patient with atrial fibrillation (AF) in whom a left atrial (LA) thrombus might have formed during laparotomy despite bridging anticoagulation therapy. No evidence of thrombus was detected by transesophageal echocardiography (TEE) at the start of surgery; however, a thrombus measuring 13 × 10 mm was found in the LA appendage by the end of the procedure, suggesting that thrombus might develop intraoperatively in patients with AF even when bridging anticoagulation is properly established. Intraoperative TEE can assist in detecting intracardiac thrombus in patients with AF regardless of their anticoagulation status and provides a tool for intervention to prevent systemic embolization.

The structure of a novel insect peptide explains its Ca2+ channel blocking and antifungal activities.

Diapause-specific peptide (DSP), derived from the leaf beetle, inhibits Ca2+ channels and has antifungal activity. DSP acts on chromaffin cells of the adrenal medulla in a fashion similar to that of omega-conotoxin GVIA, a well-known neurotoxic peptide, and blocks N-type voltage-dependent Ca2+ channels. However, the amino acid sequence of DSP has little homology with any other known Ca2+ channel blockers or antifungal peptides. In this paper, we analyzed the solution structure of DSP by using two-dimensional 1H nuclear magnetic resonance and determined the pairing of half-cystine residues forming disulfide bonds. The arrangement of the three disulfide bridges in DSP was distinct from that of other antifungal peptides and conotoxins. The overall structure of DSP is compact due in part to the three disulfide bridges and, interestingly, is very similar to those of the insect- and plant-derived antifungal peptides. On the other hand, the disulfide arrangement and the three-dimensional structure of DSP and GVIA are not similar. Nevertheless, some surface residues of DSP superimpose on the key functional residues of GVIA. This homologous distribution of hydrophobic and charged side chains may result in the functional similarity between DSP and GVIA. Thus, we propose here that the three-dimensional structure of DSP can explain its dual function as a Ca2+ channel blocker and antifungal peptide.