Glycosaminoglycans and Fibrillar Polymorphism

Research output: Contribution to book/anthology/report/proceedingBook chapterResearchpeer-review

  • Kirsten G. Malmos, Department of Molecular Biology and Genetics (MBG), Aarhus University, Aarhus, Denmark Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus, Denmark.
  • ,
  • Daniel E. Otzen

Glycosaminoglycans (GAGs) have been known since the 1980s to co-localize with amyloid deposits, yet many questions remain unanswered with regard to their interactions with amyloid. This chapter focuses on the molecular and biophysical aspects of these interactions. The interactions between GAGs and protein are believed to be mainly electrostatic in nature, involving GAG sulfate moieties which are proposed to bind the basic amino acids in a stoichiometric fashion, leaving the mature complex electrically neutral. It remains unclear whether GAGs protect the cell from toxic oligomers formed prior to the mature fibrils or rather increase the formation of aggregated species, leading to increased toxicity. Besides accelerating fibrillation in amyloidogenic proteins, GAGs have also been found to induce amyloid formation in non-amyloidogenic proteins as a possible storage-and-release switch. Thus, GAG-amyloid interactions may be both beneficial and pathologic. Clearly, there is scope for more research to address these intriguing molecular aspects.

Original languageEnglish
Title of host publicationBio-nanoimaging : Protein Misfolding and Aggregation
Number of pages10
PublisherElsevier Inc.
Publication year1 Nov 2013
ISBN (print)9780123944313
Publication statusPublished - 1 Nov 2013

    Research areas

  • Amyloid, Bio-polyanions, Co-localization, Electrostatics, Fibrils, Glycosaminoglycans, Heparan sulfate, Heparin, Protein aggregation, Proteoglycan, Sulfation

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