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Abstract

Amyloid fibrils are found in similar to 25 different diseases, including Alzheimer's disease. Lung surfactant protein C (SP-C) forms fibrils in association with pulmonary disease. It was recently found that the C-terminal domain of proSP-C (CTC), which is localized to the endoplasmic reticulum (ER) lumen, protects the transmembrane (TM) part of (pro)SP-C from aggregation into amyloid until it has a folded into an alpha-helix. CTC appears to have a more general anti-amyloid effect by also acting on TM regions of other proteins. Here we investigate interactions of CTC with the amyloid beta-peptide (A beta) associated with Alzheimer's disease and medin, a peptide that forms fibrils in the most common form of human amyloid. CTC prevents fibril formation in A beta and medin and forms a complex with A beta oligomers, as judged by size-exclusion chromatography and electrospray ionization mass spectrometry. These data suggest that CTC functions as a chaperone that acts preferentially against unfolded TM segments and structural motifs found during amyloid fibril formation, a mechanism that may be exploited in forming a basis for future anti-amyloid therapy.

Published in

Biochemistry
2009, volume: 48, number: 17, pages: 3778-3786
Publisher: AMER CHEMICAL SOC

SLU Authors

UKÄ Subject classification

Biochemistry
Molecular Biology

Publication identifier

  • DOI: https://doi.org/10.1021/bi900135c

Permanent link to this page (URI)

https://res.slu.se/id/publ/44598