We demonstrate the potential of the NanoSPR (nanoscale surface plasmon resonance sensors) method as a simple and cheap tool for the quantitative study of membrane protein-protein interactions. We use NanoSPR to determine the effectiveness of two potential drug candidates that inhibit the protein complex formation between FtsA and ZipA at initial stages of bacterial division. As the NanoSPR method relies on individual gold nanorods as sensing elements, there is no need for fluorescent labels or organic cosolvents, and it provides intrinsically high statistics. NanoSPR could become a powerful tool in drug development, drug delivery, and membrane studies.

We present muon spin relaxation (μSR) measurements of the S = 3/2 undistorted triangular lattice established in RbAg 2 Cr[VO 4 ] 2. The zero-(ZF) and longitudinal-field μSR spectra evidence the absence of spin freezing and long-range magnetic ordering down to T = 25 mK, supporting the formation of a dynamic ground state. Noticeably, we observe an anomalous temperature dependence of the ZF muon spin relaxation rate λ ZF (T), featuring a decrease below T = 20 K. This suggests the alteration of the dominant relaxation mechanism by the development of short-range magnetic correlations. A subsequent leveling off of λ ZF (T) below T = 2 K indicates persistent spin dynamics and reveals the presence of exotic magnetic excitations. The field dependence of the muon spin relaxation rate at T = 25 mK is well described by a diffusive spin transport model with algebraic spin-spin correlations. The suppressed long-range order and the peculiar temperature-dependent behavior of λ ZF (T) will be discussed in terms of the exchange interaction between Cr 3+ moments via nonmagnetic [VO 4 ] 3− entities. In the title compound, the degeneracy of the t 2g-orbital set is not lifted by a space group symmetry reduction or subject to significant anisotropy resulting from spin-orbit coupling.

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