title: Peptide amyloid surface display.
abstract: Homomeric self-assembly of peptides into amyloid fibers is a feature of many diseases. A central role has been suggested for the lateral fiber surface affecting gains of toxic function. To investigate this, a protein scaffold that presents a discrete, parallel β-sheet surface for amyloid subdomains up to eight residues in length has been designed. Scaffolds that present the fiber surface of islet amyloid polypeptide (IAPP) were prepared. The designs show sequence-specific surface effects apparent in that they gain the capacity to attenuate rates of IAPP self-assembly in solution and affect IAPP-induced toxicity in insulin-secreting cells.
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University , 260 Whitney Avenue, New Haven, Connecticut 06520-8114, United States.
authors.forename: Marisa A
authors.initials: MA
authors.lastname: Rubio
authors.forename: Diana E
authors.initials: DE
authors.lastname: Schlamadinger
authors.forename: Ellen M
authors.initials: EM
authors.lastname: White
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Miranker
mesh_terms: D000818:Animals; D002417:Cattle; D045744:Cell Line, Tumor; D006801:Humans; D058228:Islet Amyloid Polypeptide / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D010455:Peptides / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D051381:Rats; D012710:Serum Albumin, Bovine / Q000494:pharmacology; D013499:Surface Properties / Q000187:drug effects
chemical_list: D058228:Islet Amyloid Polypeptide; D010455:Peptides; D012710:Serum Albumin, Bovine