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The soluble, globular, alpha-helix-rich peptide SipA(446-684) is a domain of a bacterial protein that binds to mammalian filamentous-actin and re-arranges the host cell's cytoskeleton. We show that adding two copies of NHBP-1, a carbon nanomaterial binding peptide, to its N-terminal can induce SipA(446-684) to polymerize and assume a fibrillar structure under physiological conditions. The fibrils formed showed thioflavine T and Congo red staining profiles that are characteristic of and specific for amyloid-like structures. The alpha-helical structure of the globular protein was retained in the fibrils, suggesting the appended NHBP-1 sequence plays a key role in the formation of cross-beta spines within the fibrils. Consistent with that idea, we observed that a synthetic NHBP-1 peptide can form an amyloid-like structure under appropriate conditions. Thus, our findings add a new subtype of amyloid-like structure formation and suggest this method of assembly could be exploited in nano-biotechnology.

Conversion of a monodispersed globular protein into an amyloid-like filament by appending an artificial peptide at the N-terminal