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Small-ring molecules occupy a sweet spot between stability and instability: compact, information-rich frameworks whose reactivity is often governed by the energetic penalty of ring strain. This lecture will survey practical strategies for building structurally diverse small-ring systems, then show how their intrinsic strain can be exploited as a programmable driving force for selective bond cleavage.Through case studies spanning strain-enabled ring openings, rearrangements, and catalytic transformations, we will illustrate how “stored” strain energy can be translated into otherwise difficult-to-access acyclic architectures, especially motifs featuring adjacent stereocenters.We will focus on selective C–C bond cleavage, highlighting a predictable and robust small-ring–derived platform that controls stereochemical outcomes in SN1-type processes initiated by strain-release ring-opening chemistry.

Identifying and quantifying proteins in complex biological samples is a central challenge in research in the life sciences. Over the past two decades, mass spectrometry (MS)–based proteomics has become the central technology to achieve this on a large-scale. While the MS methods are standard and robust, the typical experimental design can be modified to obtain additional and complementary information from the biological samples. In this presentation, I will present alternative MS-based proteomics methodologies developed in our unit to address diverse biological challenges, including genome annotation, antibody sequencing, redox state determination and microbiome analysis.