NR ALJA
AU Takahashi,Y.; Ueno,A.; Mihara,H.
TI Optimization of hydrophobic domains in peptides that undergo transformation from alpha-helix to beta-fibril
QU Bioorganic and Medicinal Chemistry 1999 Jan; 7(1): 177-85
PT journal article
AB Recent studies on peptide fibrillogenesis by the de novo method as well as amyloidogenic proteins including prion proteins and Alzheimer's beta-peptides have provided insights into the conformational changes, such as alpha-helix to beta-structure, involved in folding and misfolding processes. We have found that an exposed hydrophobic nucleation domain at N-terminal causes a structural transition of a peptide from alpha-helix to beta-fibril. It became clear that N-terminal acyl groups of particular lengths in a 2alpha-helix peptide caused the peptide to undergo an alpha-to-beta transition. The peptide with the octanoyl group (C8-2alpha) showed the highest rate of transformation. The study of the designed peptides revealed that these alpha-to-beta transitions were closely related to the initial alpha-helix conformation and its stability. Engineering peptides that undergo alpha-to-beta transitions are attractive not only to the study of pathogenic proteins such as prion proteins, but also to the control of self-assembly of peptides, which will lead to the development of peptidyl self-assembling materials.
MH Amino Acid Sequence; Amyloid beta-Protein/*chemistry/ultrastructure; Chromatography, Gel; Circular Dichroism; Detergents/pharmacology; Microscopy, Electron; Molecular Sequence Data; Peptides/*chemistry; Protein Denaturation; *Protein Structure, Secondary; Support, Non-U.S. Gov't
AD Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
SP englisch
PO England