A variety of RiPPs (ribosomally synthesized and posttranslationally modified peptides) have been isolated in recent years due to their ability to quickly and accurately predict chemical structures from genomic sequences, making them more accessible for prediction than natural compounds such as terpenes and alkaloids. 1 These RiPPs, synthesized by ribosomes and subsequently generated by diverse tailoring enzymes, exhibit intriguing structures and biological activities. Among the natural products of these RiPPs, highly strained structures and those containing peculiar biaryl linkages are frequently observed. Micitide 982 (1), isolated in 2023, is a novel cyclic peptide belonging to the RiPPs class (Figure ). Structurally, it consists of three amino acid residues, namely L-tyrosine, L-proline, and L-tryptophan, forming a highly strained atrop-Tyr-Trp linkage with a cyclic peptide structure. The atropisomerism of micitide 982 (1) was determined through various techniques, including electronic circular dichroism (ECD) spectrum, NOESY spectrum, various NMR experiments, and computational chemistry. Micitide 982 (1) was isolated from a 10 L of fermentation of a bacterial strain expressing the precursor peptide and P450 for its biosynthesis, yielding 5 mg of the compound. However, due to its limited quantity, the biological activity of micitide 982 (1) remains unknown. Furthermore, the highly strained atrop-Tyr-Trp linkage, composed of the three amino acid residues in micitide 982 (1), is also found in pseudosporamide (2), which was isolated in 2020. In this study, a new and convenient synthesis route for the highly strained atrop-Tyr-Trp linkage using ligand-enabled carboxylate-directed C-H activation and subsequent atroposelective Larock macrocyclization was developed. This modular synthesis approach enabled the first total synthesis of micitide 982 (1) and facilitated the straightforward large-scale synthesis of its analogs.