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Atrial fibrillation is a disease with a complex pathophysiology, whose occurrence and persistence are caused not only by aberrant electrical signaling in the heart, but by the development of a susceptible heart substrate. These changes, such as the accumulation of adipose tissue and interstitial fibrosis, are characterized by the presence of inflammation. <i>N</i>-glycans have shown great promise as biomarkers in different diseases, specifically those involving inflammatory changes. To assess the changes in the <i>N</i>-glycosylation of the plasma proteins and IgG in atrial fibrillation, we analyzed the <i>N</i>-glycosylation of 172 patients with atrial fibrillation, before and six months after a pulmonary vein isolation procedure, with 54 cardiovascularly healthy controls. An analysis was performed using ultra-high-performance liquid chromatography. We found one oligomannose <i>N</i>-glycan structure from the plasma <i>N</i>-glycome and six IgG <i>N</i>-glycans, mainly revolving around the presence of bisecting <i>N</i>-acetylglucosamine, that were significantly different between the case and control groups. In addition, four plasma <i>N</i>-glycans, mostly oligomannose structures and a derived trait that was related to them, were found to be different in the patients who experienced an atrial fibrillation recurrence during the six-month follow-up. IgG <i>N</i>-glycosylation was extensively associated with the CHA₂DS₂-VASc score, confirming its previously reported associations with the conditions that make up the score. This is the first study looking at the <i>N</i>-glycosylation patterns in atrial fibrillation and warrants further investigation into the prospect of glycans as biomarkers for atrial fibrillation.