Structure and stability of amyloid fibrils formed from synthetic beta-peptides.
Synthetic peptides capable of self-assembling into amyloid-like fibrillar structures are emerging as novel building blocks for biomaterials. They also serve as simple model systems to study the aggregation process involved in amyloid diseases. In this paper, we probe the structure and stability of fibrillar assemblies formed by two designed peptides P11-I (CH3-CO-Q2RQ5EQ2-NH2) and P11-II (CH3-CO-Q2RFQWQFEQ2-NH2). Our results suggest that the two peptides assemble by fundamentally different mechanisms to structures of different morphologies. Coulombic interactions between charged residues Arginine and Glutamate drive the self-assembly process for peptide P11-I while the hydrophobic effect appears to be the main driving force in the self-assembly of peptide P11-II.
Department of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, California 93106-9510, USA.
Giovanni
G
Bellesia
Joan-Emma
JE
Shea
D000544:Alzheimer Disease / Q000473:pathology; D000595:Amino Acid Sequence; D000682:Amyloid / Q000096:biosynthesis / Q000737:chemistry*; D003924:Diabetes Mellitus, Type 2 / Q000473:pathology; D006801:Humans; D010300:Parkinson Disease / Q000473:pathology; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D014961:X-Ray Diffraction
D000682:Amyloid; D010455:Peptides