Common properties of Alzheimer’s amyloid-beta and a beta-solenoid hemoglobin protease of E. coli

Peter Kempen
Master Biomedical sciences thesis

For more info or word document: peterkempen @ hotmail.com (remove spaces)

Chapter 1
Introduction. 4
Amyloid-beta. 4
Hbp. 5
Common properties. 7
Chapter 2 beta-structures. 8
Chapter 3 the beta solenoid Hbp. 11
Coil shape. 11
Oligomerisation. 11
Beta-arcs. 13
Internal environment 16
Handedness. 17
Twist 17
Beta-structure formation. 18
Chaper 4. Alzheimer beta-amyloid. 19
Model for Ab40. 19
Ab42 model 22
Fibrillisation. 25
Steric zipper 26
Interacting residues. 27
Chapter 5. Common properties. 28
Cross sectional shape. 29
Handedness and Twist 30
Arches. 31
Amino acid composition. 31
Formation the beta-structure. 34
Abbreviations. 35
References. 36. 36

Abstract

Peritonitis and Alzheimer do not seem to have any overlap. On a molecular basis, where Hemoglobin protease (Hbp) and Amyloid-beta (Ab) form the main problem, they are related by forming beta-structures. Both were found to have cross-beta structures. They contain parallel beta-sheets formed by stacks of beta-strands. In Hbp this is a helical beta-structure, in Ab this is stacks of monomers that form the sheets.
The structure of Hbp has been determined for many years now. More exiting are the systematic analyses that have been done on the protein family of beta-solenoids. With this the functions and specifications of the beta-helical structure can be determined.

The molecular model for Ab has been unclear for many years due to the nature of a fibril. It has been difficult to determine the structural model with standard techniques. Recently, Japanese research showed progress by use of proline mutagenesis. This gave a more detailed construction of the monomers in the fibrillated form.
A combination of this information and systematic research on beta-solenoids can be used to predict structures and gain new research questions for investigation. Several structural elements can be used to describe the properties of fibrillating proteins; parallel or antiparallel beta-sheets, cross sectional shape, arc (turn) type, amino acid ladders, twist, handedness and type of steric zippers. These will be discussed in this review.

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