NDLI: Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis

Content Provider	PubMed Central
Author	Fernández, Ariel Berry, R. Stephen
Copyright Year	2003
Abstract	We noticed that disease-related amyloidogenic proteins and especially cellular prion proteins have the highest proportion of incompletely desolvated backbone H bonds among soluble proteins. Such bonds are vulnerable to water attack and thus represent structural weaknesses. We have measured the adsorption of proteins onto phospholipid bilayers and found a strong correlation between the extent of underwrapping of backbone H bonds in the native structure of a protein and its extent of deposition on the bilayer: the less the H bond wrapping, the higher the propensity for protein–bilayer binding. These observations support the proposition that soluble proteins with amyloidogenic propensity and membrane proteins share a pervasive building motif: the underwrapped H bonds. Whereas in membrane proteins, this motif does not signal a structural vulnerability, in soluble proteins, it is responsible for their reactivity.
Related Links	http://dx.doi.org/10.1073/pnas.0335642100
Ending Page	2396
Page Count	6
Starting Page	2391
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	5
Volume Number	100
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2003-03-04
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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