Serinetreoniini

Serinetreoniini is a fictional chemical compound described in hypothetical biochemistry and worldbuilding literature as a non-proteinogenic amino acid analog that fuses features of serine and threonine. It is depicted as a tool for exploring protein phosphorylation and kinase specificity in imagined research settings.

In the portrayed structure, serinetreoniini is a small, highly polar molecule that can exist as a zwitterion at physiological pH. It has an alpha-amino group and an alpha-carboxylate, with a side chain bearing a hydroxyl-bearing moiety reminiscent of serine and threonine. Its properties are described as compatible with aqueous environments and typical of amino acid–like substrates, though it is not reported to occur naturally.

In fiction, synthesis is depicted as involving standard protective-group chemistry applied to serine- and threonine-like fragments, followed by selective side-chain modification to introduce a second hydroxyl group. The compound is portrayed as not occurring naturally and as being available only from specialized laboratories in the fictional world.

Proposed uses include serving as a substrate analogue for serine/threonine kinases, acting as a competitive inhibitor of phosphorylation, or enabling selective labeling of phosphorylation sites in proteins. In stories and hypothetical research, serinetreoniini helps explore signaling pathways and enzyme specificity, providing a conceptual tool for discussing protein modification.

In real-world terms, serinetreoniini has no existence in empirical chemistry or pharmacology, and there is no regulatory status or safety data. If encountered in real laboratories, it is treated as a hypothetical compound; otherwise, it serves as a narrative device for worldbuilding and academic speculation.