Effects of DHLA-capped CdSe/ZnS quantum dots on the fibrillation of human serum albumin

Charles H. Vannoy, Roger Leblanc

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

Nanoparticles (NPs) are extremely small in size and possess very large surface areas, which gives them unique properties and applications distinct from those of bulk systems. When exposed to biological fluid, these NPs may become coated with proteins and other biomolecules given their dynamic nature. Hence, there is a significant possibility of an enhanced rate of protein fibrillation by utilizing the NPs as nucleation centers and, thus, promoting fibril formation. Protein fibrillation is closely associated with many fatal human diseases, including neurodegenerative diseases and a variety of systemic amyloidoses. This topic of protein-NP interaction brings about many key issues and concerns, especially with respect to the potential risks to human health and the environment. Herein, we demonstrate the effects of specific NPs, semiconductor quantum dots (QDs), in the process of protein fibril formation from samples of human serum albumin (HSA). The protein - NP systems are analyzed by time-lapse Thioflavin T spectroscopy, Congo red binding assays, circular dichroism (CD), protein fluorescence spectroscopy, and transmission electron microscopy (TEM). Our experimental results illustrate that an increased rate of fibrillation occurs following a thermally activated mechanism in conjunction with the addition of NPs into the protein system. These results give rise to the understanding and possibility of controlling biological self-assembly processes for use in nanobiotechnology and nanomedicine.

Original languageEnglish
Pages (from-to)10881-10888
Number of pages8
JournalJournal of Physical Chemistry B
Volume114
Issue number33
DOIs
StatePublished - Aug 26 2010

Fingerprint

8,11,14-Eicosatrienoic Acid
fibrillation
albumins
Serum Albumin
serums
Semiconductor quantum dots
quantum dots
proteins
Proteins
Nanoparticles
nanoparticles
Nanobiotechnology
Neurodegenerative diseases
Medical nanotechnology
Congo Red
Fluorescence spectroscopy
Dichroism
Biomolecules
Self assembly
spectroscopy

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Materials Chemistry
  • Surfaces, Coatings and Films

Cite this

Effects of DHLA-capped CdSe/ZnS quantum dots on the fibrillation of human serum albumin. / Vannoy, Charles H.; Leblanc, Roger.

In: Journal of Physical Chemistry B, Vol. 114, No. 33, 26.08.2010, p. 10881-10888.

Research output: Contribution to journalArticle

@article{10ccaddd00a74d2897c96145f8445119,
title = "Effects of DHLA-capped CdSe/ZnS quantum dots on the fibrillation of human serum albumin",
abstract = "Nanoparticles (NPs) are extremely small in size and possess very large surface areas, which gives them unique properties and applications distinct from those of bulk systems. When exposed to biological fluid, these NPs may become coated with proteins and other biomolecules given their dynamic nature. Hence, there is a significant possibility of an enhanced rate of protein fibrillation by utilizing the NPs as nucleation centers and, thus, promoting fibril formation. Protein fibrillation is closely associated with many fatal human diseases, including neurodegenerative diseases and a variety of systemic amyloidoses. This topic of protein-NP interaction brings about many key issues and concerns, especially with respect to the potential risks to human health and the environment. Herein, we demonstrate the effects of specific NPs, semiconductor quantum dots (QDs), in the process of protein fibril formation from samples of human serum albumin (HSA). The protein - NP systems are analyzed by time-lapse Thioflavin T spectroscopy, Congo red binding assays, circular dichroism (CD), protein fluorescence spectroscopy, and transmission electron microscopy (TEM). Our experimental results illustrate that an increased rate of fibrillation occurs following a thermally activated mechanism in conjunction with the addition of NPs into the protein system. These results give rise to the understanding and possibility of controlling biological self-assembly processes for use in nanobiotechnology and nanomedicine.",
author = "Vannoy, {Charles H.} and Roger Leblanc",
year = "2010",
month = "8",
day = "26",
doi = "10.1021/jp1045904",
language = "English",
volume = "114",
pages = "10881--10888",
journal = "Journal of Physical Chemistry B Materials",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "33",

}

TY - JOUR

T1 - Effects of DHLA-capped CdSe/ZnS quantum dots on the fibrillation of human serum albumin

AU - Vannoy, Charles H.

AU - Leblanc, Roger

PY - 2010/8/26

Y1 - 2010/8/26

N2 - Nanoparticles (NPs) are extremely small in size and possess very large surface areas, which gives them unique properties and applications distinct from those of bulk systems. When exposed to biological fluid, these NPs may become coated with proteins and other biomolecules given their dynamic nature. Hence, there is a significant possibility of an enhanced rate of protein fibrillation by utilizing the NPs as nucleation centers and, thus, promoting fibril formation. Protein fibrillation is closely associated with many fatal human diseases, including neurodegenerative diseases and a variety of systemic amyloidoses. This topic of protein-NP interaction brings about many key issues and concerns, especially with respect to the potential risks to human health and the environment. Herein, we demonstrate the effects of specific NPs, semiconductor quantum dots (QDs), in the process of protein fibril formation from samples of human serum albumin (HSA). The protein - NP systems are analyzed by time-lapse Thioflavin T spectroscopy, Congo red binding assays, circular dichroism (CD), protein fluorescence spectroscopy, and transmission electron microscopy (TEM). Our experimental results illustrate that an increased rate of fibrillation occurs following a thermally activated mechanism in conjunction with the addition of NPs into the protein system. These results give rise to the understanding and possibility of controlling biological self-assembly processes for use in nanobiotechnology and nanomedicine.

AB - Nanoparticles (NPs) are extremely small in size and possess very large surface areas, which gives them unique properties and applications distinct from those of bulk systems. When exposed to biological fluid, these NPs may become coated with proteins and other biomolecules given their dynamic nature. Hence, there is a significant possibility of an enhanced rate of protein fibrillation by utilizing the NPs as nucleation centers and, thus, promoting fibril formation. Protein fibrillation is closely associated with many fatal human diseases, including neurodegenerative diseases and a variety of systemic amyloidoses. This topic of protein-NP interaction brings about many key issues and concerns, especially with respect to the potential risks to human health and the environment. Herein, we demonstrate the effects of specific NPs, semiconductor quantum dots (QDs), in the process of protein fibril formation from samples of human serum albumin (HSA). The protein - NP systems are analyzed by time-lapse Thioflavin T spectroscopy, Congo red binding assays, circular dichroism (CD), protein fluorescence spectroscopy, and transmission electron microscopy (TEM). Our experimental results illustrate that an increased rate of fibrillation occurs following a thermally activated mechanism in conjunction with the addition of NPs into the protein system. These results give rise to the understanding and possibility of controlling biological self-assembly processes for use in nanobiotechnology and nanomedicine.

UR - http://www.scopus.com/inward/record.url?scp=77955898208&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77955898208&partnerID=8YFLogxK

U2 - 10.1021/jp1045904

DO - 10.1021/jp1045904

M3 - Article

C2 - 20681557

AN - SCOPUS:77955898208

VL - 114

SP - 10881

EP - 10888

JO - Journal of Physical Chemistry B Materials

JF - Journal of Physical Chemistry B Materials

SN - 1520-6106

IS - 33

ER -