The materials science of protein aggregation

D. L. Cox, H. Lashuel, K. Y.C. Lee, R. R.R. Singh

Research output: Contribution to journalReview article

17 Citations (Scopus)


Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer's, Parkinson's, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig's disease), Huntington's, and type II (mature onset) diabetes. In many cases, it has been demonstrated that conformational change and aggregation can occur outside living cells and complex biochemical networks. Hence, approaches from materials and physical science have enhanced our understanding of the role of protein aggregation in these diseases at the molecular and nanoscale levels. In this article, we will review what is known about these protein structures from the perspective of materials science, focusing on the details of emergent oligomeric and nanotube-like structures, their interactions with model lipid bilayers, how the structures relate to observed biological phenomena, and how protein aggregation and amyloid formation can be employed for the good in biology and materials science.

Original languageEnglish
Pages (from-to)452-457
Number of pages6
JournalMRS Bulletin
Issue number6
Publication statusPublished - Jun 2005



  • Amyloid diseases
  • Complex adaptive matter
  • Emergent behavior
  • Nanotubes
  • Nanowires
  • Prion diseases
  • Protein aggregation
  • Protofibrils

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Physical and Theoretical Chemistry

Cite this

Cox, D. L., Lashuel, H., Lee, K. Y. C., & Singh, R. R. R. (2005). The materials science of protein aggregation. MRS Bulletin, 30(6), 452-457.