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Cataract is one of the most prevalent protein aggregation disorders and stillthe biggest cause of vision loss worldwide. The human lens, in its core region,lacks turnover of any cells or cellular components; it has therefore evolvedremarkable mechanisms for resisting protein aggregation for a lifetime. We nowreport that one such mechanism relies on an unusually abundant metabolite,myo-inositol, to suppress light-scattering aggregation of lens proteins. Wequantified aggregation suppression by in vitro turbidimetry and characterizedboth macroscopic and microscopic mechanisms of myo-inositol action usingnegative-stain electron microscopy, differential scanning fluorometry, and athermal scanning Raman spectroscopy apparatus. Given recent metabolomicevidence that it is dramatically depleted in human cataractous lenses comparedto age-matched controls, we suggest that maintaining or restoring healthylevels of myo-inositol in the lens may be a simple, safe, and widely availablestrategy for reducing the global burden of cataract.

A native chemical chaperone in the human eye lens