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However, the molecular mechanism of their function is not well understood. Using solution\u2010state and solid\u2010state NMR spectroscopy in combination with ensemble\u2010averaged dynamics simulations and other biophysical methods including TEM, fluorescence spectroscopy and microscopy, and DLS, we characterize ISM structural preferences and interactions. We find that the ISM peptide R3\u2010GI is highly dynamic, can adopt a \u03b2\u2010like structure, and oligomerizes into colloid\u2010like assemblies in a process that is reminiscent of liquid\u2013liquid phase separation (LLPS). Our results suggest that such assemblies yield multivalent surfaces for interactions with A\u03b240. 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