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© The Rockefeller University Press, 0021-9525/2003/5/461 $5.00
The Journal of Cell Biology, Volume 161, Number 3, 461-462

Amyloid as a natural product

¹ Department of Chemistry and The Skaggs Institute of Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037
² Department of Cell Biology and the Institute for Childhood and Neglected Diseases, The Scripps Research Institute, La Jolla, CA 92037

Address correspondence to J.W. Kelly, Department of Chemistry and The Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: (858) 784-9601. Fax: (858) 784-9610. E-mail: jkelly{at}scripps.edu; or W.E. Balch, Department of Cell Biology and the Institute for Childhood and Neglected Diseases, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: (858) 784-2310. Fax: (858) 784-9196. E-mail: webalch{at}scripps.edu

Amyloid fibrils, such as those found in Alzheimer's and the gelsolin amyloid diseases, result from the misassembly of peptides produced by either normal or aberrant intracellular proteolytic processing. A paper in this issue by Marks and colleagues (Berson et al., 2003) demonstrates that intra-melanosome fibrils are formed through normal biological proteolytic processing of an integral membrane protein. The resulting peptide fragment assembles into fibrils promoting the formation of melanin pigment granules. These results, along with the observation that amyloid fibril formation by bacteria is highly orchestrated, suggest that fibril formation is an evolutionary conserved biological pathway used to generate natural product nanostructures.

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