NDLI: Aggregation of proteins with expanded glutamine and alaninerepeats of the glutamine-rich and asparagine-rich domains of Sup35 andof the amyloid β-peptide of amyloid plaques

Content Provider	PubMed Central
Author	Perutz, M. F. Pope, B. J. Owen, D. Wanker, E. E. Scherzinger, E.
Copyright Year	2002
Abstract	The exon-1 peptide of huntingtin has 51 Gln repeats andproduces the symptoms of Huntington's disease in transgenic mice.Aggregation of the yeast Sup35 protein into prions has been attributedto its glutamine-rich and asparagine-rich domain. Here, we show thatpoly-l-asparagine forms polar zippers similar to those ofpoly-l-glutamine. In solution at acid pH, theglutamine-rich and asparagine-rich 18-residue Sup35 peptide, renderedsoluble by the addition of two aspartates at the amino end and twolysines at the carboxyl end, gives a β-sheet CD spectrum; itaggregates at neutral pH. A poly-alanine peptideD2A10K2 gives an α-helical CDspectrum at all pHs and does not aggregate; a peptide with the sequenceof the C-terminal helix of the α-chain of human hemoglobin, precededby two aspartates and followed by two lysines, exhibits a random coilspectrum and does not aggregate either. Alignment of severalβ-strands with the sequence of the 42-residue Alzheimer's amyloidβ-peptide shows that they can be linked together by a network of saltbridges. We also asked why single amino acid replacements can sodestabilize the native structures of proteins that they unfold and formamyloids. The difference in free energy of a protein molecule betweenits native, fully ordered structure and an amorphous mixture ofrandomly coiled chains is only of the order of 10 kcal/mol.Theory shows that destabilization of the native structureby no more than 2 kcal/mol can increase the probability of nucleationof disordered aggregates from which amyloids could grow130,000-fold.
Related Links	http://dx.doi.org/10.1073/pnas.042681599
Ending Page	5600
Page Count	5
Starting Page	5596
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	8
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-04-16
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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