Abstract
‘Amyloid binging proteins’ is a generic term used to designate proteins that interact with different forms of amyloidogenic peptides or proteins and that, as a result, may modulate their physiological and pathological functions by altering solubility, transport, clearance, degradation, and fibril formation. We describe a simple affinity chromatography protocol to isolate and characterize amyloid-binding proteins based on the use of sequential elution steps that may provide further information on the type of binding interaction. As an example, we depict the application of this protocol to the study of Alzheimer’s amyloid β (Aβ) peptide-binding proteins derived from human plasma. Biochemical analysis of the proteins eluted under different conditions identified serum amyloid P component (SAP) and apolipoprotein J (clusterin) as the main plasma Aβ-binding proteins while various apolipoproteins (apoA-IV, apoE, and apoA-I), as well as albumin (HSA) and fibulin were identified as minor contributors.
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Abbreviations
- ACT:
-
α1-Antichymotrypsin
- AD:
-
Alzheimer’s disease
- apoA-I:
-
Apolipoprotein A-I
- apoA-IV:
-
Apolipoprotein A-IV
- apoE:
-
Apolipoprotein E
- apoJ:
-
Apolipoprotein J (clusterin)
- CAPS:
-
3-Cyclohexilamino-1-propanesulphonic acid
- CNBr:
-
Cyanogen bromide
- ELISA:
-
Enzyme-linked immunosorbent assay
- HSA:
-
Human serum albumin
- NHS:
-
N-hydroxysuccinimide
- SAP:
-
Serum amyloid P component
- Vn:
-
Vitronectin
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Acknowledgments
This work was supported by grants from the Fundación CIEN-ISCIII (MPY 1308/08) and CIBERNED to MC and from the National Institutes of Health NS051715 to AR and AG030539 to JG.
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Calero, M., Rostagno, A., Ghiso, J. (2012). Search for Amyloid-Binding Proteins by Affinity Chromatography. In: Sigurdsson, E., Calero, M., Gasset, M. (eds) Amyloid Proteins. Methods in Molecular Biology, vol 849. Humana Press. https://doi.org/10.1007/978-1-61779-551-0_15
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DOI: https://doi.org/10.1007/978-1-61779-551-0_15
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