The materials science of protein aggregation

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

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

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
Volume30
Issue number6
Publication statusPublished - 1 Jun 2005
Externally publishedYes

Fingerprint

Materials science
materials science
Agglomeration
proteins
Proteins
Advanced Launch System (STS)
Parkinson disease
physical sciences
biology
Lipid bilayers
Prions
lipids
nanotubes
Medical problems
Amyloid
Nanotubes
Cells
interactions

Keywords

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

ASJC Scopus subject areas

  • Materials Science(all)
  • Physics and Astronomy (miscellaneous)

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.

The materials science of protein aggregation. / Cox, D. L.; Lashuel, H.; Lee, K. Y C; Singh, R. R R.

In: MRS Bulletin, Vol. 30, No. 6, 01.06.2005, p. 452-457.

Research output: Contribution to journalArticle

Cox, DL, Lashuel, H, Lee, KYC & Singh, RRR 2005, 'The materials science of protein aggregation', MRS Bulletin, vol. 30, no. 6, pp. 452-457.
Cox DL, Lashuel H, Lee KYC, Singh RRR. The materials science of protein aggregation. MRS Bulletin. 2005 Jun 1;30(6):452-457.
Cox, D. L. ; Lashuel, H. ; Lee, K. Y C ; Singh, R. R R. / The materials science of protein aggregation. In: MRS Bulletin. 2005 ; Vol. 30, No. 6. pp. 452-457.
@article{5d1d9c69b7984e88ab55858b57e6295d,
title = "The materials science of protein aggregation",
abstract = "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.",
keywords = "Amyloid diseases, Complex adaptive matter, Emergent behavior, Nanotubes, Nanowires, Prion diseases, Protein aggregation, Protofibrils",
author = "Cox, {D. L.} and H. Lashuel and Lee, {K. Y C} and Singh, {R. R R}",
year = "2005",
month = "6",
day = "1",
language = "English",
volume = "30",
pages = "452--457",
journal = "MRS Bulletin",
issn = "0883-7694",
publisher = "Materials Research Society",
number = "6",

}

TY - JOUR

T1 - The materials science of protein aggregation

AU - Cox, D. L.

AU - Lashuel, H.

AU - Lee, K. Y C

AU - Singh, R. R R

PY - 2005/6/1

Y1 - 2005/6/1

N2 - 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.

AB - 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.

KW - Amyloid diseases

KW - Complex adaptive matter

KW - Emergent behavior

KW - Nanotubes

KW - Nanowires

KW - Prion diseases

KW - Protein aggregation

KW - Protofibrils

UR - http://www.scopus.com/inward/record.url?scp=33744795434&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33744795434&partnerID=8YFLogxK

M3 - Article

VL - 30

SP - 452

EP - 457

JO - MRS Bulletin

JF - MRS Bulletin

SN - 0883-7694

IS - 6

ER -