Cannabinoids, particularly those derived from cannabis, have attracted considerable attention in recent years for their therapeutic potential in treating various diseases and ailments. In this study, we identified cannabinoid byproducts that result from the combustion of cannabidiol (CBD) - henceforth referred to as pyrocannabinoids - and employed molecular docking simulations to investigate their interactions with key protein targets implicated in different physiological processes. Specifically, we focused on peroxisome proliferator-activated receptor gamma (PPAR-γ), p21-activated kinase 1 (PAK1), CB1, CB2, and GPR119 proteins, elucidating the binding modes and affinities of pyrocannabinoid byproducts to these receptors. This investigation was done in collaboration with Real Isolates LLC. Our findings revealed diverse ligand-protein interactions, with some pyrocannabinoids displaying favorable binding energies and stable ligand-protein complexes. However, variations in binding affinities across different proteins underscored the complex pharmacological profiles of the pyrocannabinoids. Furthermore, the prediction of adsorption, distribution, metabolism, excretion and toxicity (ADMET) properties highlighted both promising and concerning aspects of cannabinoid pharmacokinetics, emphasizing the need for thorough preclinical evaluation. Additionally, our investigation into potential metabolic sites using cytochrome P450 enzymes provided insights into cannabinoid metabolites. Overall, our study contributes to the understanding of pyrocannabinoid pharmacology and informs the rational design of pyrocannabinoid-based therapeutics. Further experimental validation is warranted to translate these findings into clinically relevant applications.