NDLI: The interaction of beta-amyloid protein fragment (12-28) with lipid environments.

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The interaction of beta-amyloid protein fragment (12-28) with lipid environments.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Fletcher, T. G. Keire, D. A.
Description	Country affiliation: United States Author Affiliation: Fletcher TG ( Beckman Research Institute, City of Hope, Duarte, California 91010-0269, USA.)
Abstract	The neurotoxicity of beta-amyloid protein (beta AP) fragments may be a result of their solution conformation, which is very sensitive to solution conditions. In this work we describe NMR and CD studies of the conformation of beta AP(12-28) in lipid (micelle) environments as a function of pH and lipid type. The interaction of beta AP(12-28) with zwitterionic dodecylphosphocholine (DPC) micelles is weak and alters the conformation when compared to water solution alone. By contrast, the interaction of the peptide with anionic sodium dodecylsulfate (SDS) micelles is strong: beta AP(12-28) is mostly bound, is alpha-helical from K16 to V24, and aggregates slowly. The pH-dependent conformation changes of beta AP(12-28) in solution occur in the pH range at which the side-chain groups of E22, D23, H13, and H14 are deprotonated (pKas ca. 4 and 6.5); the interaction of beta AP(12-28) with SDS micelles alters the pH-dependent conformational transitions of the peptide whereas the weak interaction with DPC micelles causes little change.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	3
Volume Number	6
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1997-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amyloid Beta-peptides Chemistry Lipids Peptide Fragments Amino Acid Sequence Magnetic Resonance Spectroscopy Molecular Sequence Data Protein Conformation Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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