Brain protein BASP1 forms oligomers that resemble amyloid protein oligomers in some respects, including interaction with conformation-specific antibodies against amyloid oligomers. Aggregation-prone N-terminal myristoylated peptide myr-BASP1 (1-13) forms fibrillar aggregates of amyloid-like structure under physiological conditions in vitro, which is also the evidence of BASP1 similarity to amyloid proteins. Protein cross-linking by glutaraldehyde in situ demonstrated that BASP1 exists on the presynaptic membrane as lipid raft-associated oligomers. In addition, BASP1 is non-toxic to PC12 cells, when applied either as a monomer or oligomer. We conclude that BASP1 oligomer is a non-pathological physiologically relevant functional form of this protein.
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