Nanoimaging for protein misfolding and related diseases

Yuri L Lyubchenko, Simon Sherman, Luda S. Shlyakhtenko, Vladimir N. Uversky

Research output: Contribution to journalReview article

37 Citations (Scopus)

Abstract

Misfolding and aggregation of proteins is a common thread linking a number of important human health problems. The misfolded and aggregated proteins are inducers of cellular stress and activators of immunity in neurodegenerative diseases. They might posses clear cytotoxic properties, being responsible for the dysfunction and loss of cells in the affected organs. Despite the crucial importance of protein misfolding and abnormal interactions, very little is currently known about the molecular mechanism underlying these processes. Factors that lead to protein misfolding and aggregation in vitro are poorly understood, not to mention the complexities involved in the formation of protein nanoparticles with different morphologies (e.g., the nanopores) in vivo. A better understanding of the molecular mechanisms of misfolding and aggregation might facilitate development of the rational approaches to prevent pathologies mediated by protein misfolding. The conventional tools currently available to researchers can only provide an averaged picture of a living system, whereas much of the subtle or short-lived information is lost. We believe that the existing and emerging nanotools might help solving these problems by opening the entirely novel pathways for the development of early diagnostic and therapeutic approaches. This article summarizes recent advances of the nanoscience in detection and characterization of misfolded protein conformations. Based on these findings, we outline our view on the nanoscience development towards identification intracellular nanomachines and/or multicomponent complexes critically involved in protein misfolding.

Original languageEnglish (US)
Pages (from-to)53-70
Number of pages18
JournalJournal of Cellular Biochemistry
Volume99
Issue number1
DOIs
StatePublished - Sep 1 2006

Fingerprint

Proteostasis Deficiencies
Proteins
Nanoscience
Agglomeration
Nanopores
Protein Conformation
Neurodegenerative diseases
Neurodegenerative Diseases
Nanoparticles
Pathology
Medical problems
Immunity
Conformations
Research Personnel
Health

Keywords

  • Atomic force microscopy
  • Conformational disease
  • Force spectroscopy
  • Nanomedicine
  • Protein aggregation
  • Protein misfolding
  • Single molecule analyses

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Nanoimaging for protein misfolding and related diseases. / Lyubchenko, Yuri L; Sherman, Simon; Shlyakhtenko, Luda S.; Uversky, Vladimir N.

In: Journal of Cellular Biochemistry, Vol. 99, No. 1, 01.09.2006, p. 53-70.

Research output: Contribution to journalReview article

Lyubchenko, Yuri L ; Sherman, Simon ; Shlyakhtenko, Luda S. ; Uversky, Vladimir N. / Nanoimaging for protein misfolding and related diseases. In: Journal of Cellular Biochemistry. 2006 ; Vol. 99, No. 1. pp. 53-70.
@article{3dd2106cb15b4cdb99790d2630edaaf7,
title = "Nanoimaging for protein misfolding and related diseases",
abstract = "Misfolding and aggregation of proteins is a common thread linking a number of important human health problems. The misfolded and aggregated proteins are inducers of cellular stress and activators of immunity in neurodegenerative diseases. They might posses clear cytotoxic properties, being responsible for the dysfunction and loss of cells in the affected organs. Despite the crucial importance of protein misfolding and abnormal interactions, very little is currently known about the molecular mechanism underlying these processes. Factors that lead to protein misfolding and aggregation in vitro are poorly understood, not to mention the complexities involved in the formation of protein nanoparticles with different morphologies (e.g., the nanopores) in vivo. A better understanding of the molecular mechanisms of misfolding and aggregation might facilitate development of the rational approaches to prevent pathologies mediated by protein misfolding. The conventional tools currently available to researchers can only provide an averaged picture of a living system, whereas much of the subtle or short-lived information is lost. We believe that the existing and emerging nanotools might help solving these problems by opening the entirely novel pathways for the development of early diagnostic and therapeutic approaches. This article summarizes recent advances of the nanoscience in detection and characterization of misfolded protein conformations. Based on these findings, we outline our view on the nanoscience development towards identification intracellular nanomachines and/or multicomponent complexes critically involved in protein misfolding.",
keywords = "Atomic force microscopy, Conformational disease, Force spectroscopy, Nanomedicine, Protein aggregation, Protein misfolding, Single molecule analyses",
author = "Lyubchenko, {Yuri L} and Simon Sherman and Shlyakhtenko, {Luda S.} and Uversky, {Vladimir N.}",
year = "2006",
month = "9",
day = "1",
doi = "10.1002/jcb.20989",
language = "English (US)",
volume = "99",
pages = "53--70",
journal = "Journal of Cellular Biochemistry",
issn = "0730-2312",
publisher = "Wiley-Liss Inc.",
number = "1",

}

TY - JOUR

T1 - Nanoimaging for protein misfolding and related diseases

AU - Lyubchenko, Yuri L

AU - Sherman, Simon

AU - Shlyakhtenko, Luda S.

AU - Uversky, Vladimir N.

PY - 2006/9/1

Y1 - 2006/9/1

N2 - Misfolding and aggregation of proteins is a common thread linking a number of important human health problems. The misfolded and aggregated proteins are inducers of cellular stress and activators of immunity in neurodegenerative diseases. They might posses clear cytotoxic properties, being responsible for the dysfunction and loss of cells in the affected organs. Despite the crucial importance of protein misfolding and abnormal interactions, very little is currently known about the molecular mechanism underlying these processes. Factors that lead to protein misfolding and aggregation in vitro are poorly understood, not to mention the complexities involved in the formation of protein nanoparticles with different morphologies (e.g., the nanopores) in vivo. A better understanding of the molecular mechanisms of misfolding and aggregation might facilitate development of the rational approaches to prevent pathologies mediated by protein misfolding. The conventional tools currently available to researchers can only provide an averaged picture of a living system, whereas much of the subtle or short-lived information is lost. We believe that the existing and emerging nanotools might help solving these problems by opening the entirely novel pathways for the development of early diagnostic and therapeutic approaches. This article summarizes recent advances of the nanoscience in detection and characterization of misfolded protein conformations. Based on these findings, we outline our view on the nanoscience development towards identification intracellular nanomachines and/or multicomponent complexes critically involved in protein misfolding.

AB - Misfolding and aggregation of proteins is a common thread linking a number of important human health problems. The misfolded and aggregated proteins are inducers of cellular stress and activators of immunity in neurodegenerative diseases. They might posses clear cytotoxic properties, being responsible for the dysfunction and loss of cells in the affected organs. Despite the crucial importance of protein misfolding and abnormal interactions, very little is currently known about the molecular mechanism underlying these processes. Factors that lead to protein misfolding and aggregation in vitro are poorly understood, not to mention the complexities involved in the formation of protein nanoparticles with different morphologies (e.g., the nanopores) in vivo. A better understanding of the molecular mechanisms of misfolding and aggregation might facilitate development of the rational approaches to prevent pathologies mediated by protein misfolding. The conventional tools currently available to researchers can only provide an averaged picture of a living system, whereas much of the subtle or short-lived information is lost. We believe that the existing and emerging nanotools might help solving these problems by opening the entirely novel pathways for the development of early diagnostic and therapeutic approaches. This article summarizes recent advances of the nanoscience in detection and characterization of misfolded protein conformations. Based on these findings, we outline our view on the nanoscience development towards identification intracellular nanomachines and/or multicomponent complexes critically involved in protein misfolding.

KW - Atomic force microscopy

KW - Conformational disease

KW - Force spectroscopy

KW - Nanomedicine

KW - Protein aggregation

KW - Protein misfolding

KW - Single molecule analyses

UR - http://www.scopus.com/inward/record.url?scp=33748067296&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33748067296&partnerID=8YFLogxK

U2 - 10.1002/jcb.20989

DO - 10.1002/jcb.20989

M3 - Review article

VL - 99

SP - 53

EP - 70

JO - Journal of Cellular Biochemistry

JF - Journal of Cellular Biochemistry

SN - 0730-2312

IS - 1

ER -