Late embryogenesis abundant protein (LEA protein)

Late embryogenesis abundant (LEA) proteins are a large and diverse family of highly hydrophilic, typically intrinsically disordered proteins (IDPs) that play a critical role in protecting organisms from desiccation and abiotic stress [1, 2]. Originally identified in the maturing seeds of higher plants, these proteins are also found in various bacteria and desiccation-tolerant invertebrates like tardigrades and nematodes [2, 3]. Their primary biological function involves acting as molecular shields or chaperones that prevent the aggregation of other proteins and stabilize cellular membranes and enzymes during water deficit [4, 5]. While LEA proteins are not naturally expressed in humans, they have gained significant attention in biotechnology for their potential to stabilize vaccines, therapeutic proteins, and cells during freeze-drying or cryopreservation [5, 6]. Furthermore, research has demonstrated that certain LEA proteins can inhibit the formation of toxic protein aggregates associated with human neurodegenerative diseases, such as alpha-synuclein in Parkinson's disease, in experimental models [6, 7]. Despite these promising applications, LEA proteins are not currently utilized as conventional drug targets, and no small-molecule drugs have been developed to modulate their activity [8].

Other names

LEA proteinsDehydrinMaturation proteinLate embryogenesis abundant-like proteinD-7 proteinD-11 protein

None identified; LEA proteins are not currently targeted by any approved or investigational drugs.