Lysozyme encapsulated gold nanoclusters for probing the early stage of lysozyme aggregation under acidic conditions

Research output: Contribution to journalArticle

Abstract

Protein aggregation can lead to several incurable amyloidosis diseases. The full aggregation pathway is not fully understood, creating the need for new methods of studying this important biological phenomenon. Lysozyme is an amyloidogenic protein which is often used as a model protein for studying amyloidosis. This work explores the potential of employing Lysozyme encapsulated gold nanoclusters (Ly-AuNCs) to study the protein’s aggregation. The fluorescence emission properties of Ly-AuNCs were studied in the presence of increasing concentrations of native lysozyme and as a function of pH, of relevance in macromolecular crowding and inflammation-triggered aggregation. AuNC fluorescence was observed to both redshift and increase in intensity as pH is increased or when native lysozyme is added to a solution of Ly-AuNCs at pH 3. The long (μs) fluorescence lifetime component of AuNC emission was observed to decrease under both conditions. Interestingly it was found via Time Resolved Emission Spectra (TRES) that both AuNC fluorescence components increase in intensity and redshift with increasing pH while only the long lifetime component of AuNC was observed to change when adding native lysozyme to solution; indicating that the underlying mechanisms for the changes observed are fundamentally different for each case. It is possible that the sensitivity of Ly-AuNCs to native lysozyme concentration could be utilized to study early stage aggregation.
LanguageEnglish
Article number111540
Number of pages10
JournalJournal of Photochemistry and Photobiology B: Biology
Volume197
Early online date22 Jun 2019
DOIs
Publication statusPublished - 31 Aug 2019

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lysozyme
Muramidase
nanoclusters
Gold
gold
Fluorescence
proteins
fluorescence
Amyloidosis
Amyloidogenic Proteins
Biological Phenomena
life (durability)
Proteins
crowding
emission spectra
Inflammation
sensitivity

Keywords

  • gold nanoclusters
  • lysozyme
  • protein aggregation
  • fluorescence

Cite this

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title = "Lysozyme encapsulated gold nanoclusters for probing the early stage of lysozyme aggregation under acidic conditions",
abstract = "Protein aggregation can lead to several incurable amyloidosis diseases. The full aggregation pathway is not fully understood, creating the need for new methods of studying this important biological phenomenon. Lysozyme is an amyloidogenic protein which is often used as a model protein for studying amyloidosis. This work explores the potential of employing Lysozyme encapsulated gold nanoclusters (Ly-AuNCs) to study the protein’s aggregation. The fluorescence emission properties of Ly-AuNCs were studied in the presence of increasing concentrations of native lysozyme and as a function of pH, of relevance in macromolecular crowding and inflammation-triggered aggregation. AuNC fluorescence was observed to both redshift and increase in intensity as pH is increased or when native lysozyme is added to a solution of Ly-AuNCs at pH 3. The long (μs) fluorescence lifetime component of AuNC emission was observed to decrease under both conditions. Interestingly it was found via Time Resolved Emission Spectra (TRES) that both AuNC fluorescence components increase in intensity and redshift with increasing pH while only the long lifetime component of AuNC was observed to change when adding native lysozyme to solution; indicating that the underlying mechanisms for the changes observed are fundamentally different for each case. It is possible that the sensitivity of Ly-AuNCs to native lysozyme concentration could be utilized to study early stage aggregation.",
keywords = "gold nanoclusters, lysozyme, protein aggregation, fluorescence",
author = "Nora Alkudaisi and Russell, {Ben Allan} and Birch, {David J. S.} and Yu Chen",
year = "2019",
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day = "31",
doi = "10.1016/j.jphotobiol.2019.111540",
language = "English",
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journal = "Journal of Photochemistry and Photobiology B: Biology",
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T1 - Lysozyme encapsulated gold nanoclusters for probing the early stage of lysozyme aggregation under acidic conditions

AU - Alkudaisi, Nora

AU - Russell, Ben Allan

AU - Birch, David J. S.

AU - Chen, Yu

PY - 2019/8/31

Y1 - 2019/8/31

N2 - Protein aggregation can lead to several incurable amyloidosis diseases. The full aggregation pathway is not fully understood, creating the need for new methods of studying this important biological phenomenon. Lysozyme is an amyloidogenic protein which is often used as a model protein for studying amyloidosis. This work explores the potential of employing Lysozyme encapsulated gold nanoclusters (Ly-AuNCs) to study the protein’s aggregation. The fluorescence emission properties of Ly-AuNCs were studied in the presence of increasing concentrations of native lysozyme and as a function of pH, of relevance in macromolecular crowding and inflammation-triggered aggregation. AuNC fluorescence was observed to both redshift and increase in intensity as pH is increased or when native lysozyme is added to a solution of Ly-AuNCs at pH 3. The long (μs) fluorescence lifetime component of AuNC emission was observed to decrease under both conditions. Interestingly it was found via Time Resolved Emission Spectra (TRES) that both AuNC fluorescence components increase in intensity and redshift with increasing pH while only the long lifetime component of AuNC was observed to change when adding native lysozyme to solution; indicating that the underlying mechanisms for the changes observed are fundamentally different for each case. It is possible that the sensitivity of Ly-AuNCs to native lysozyme concentration could be utilized to study early stage aggregation.

AB - Protein aggregation can lead to several incurable amyloidosis diseases. The full aggregation pathway is not fully understood, creating the need for new methods of studying this important biological phenomenon. Lysozyme is an amyloidogenic protein which is often used as a model protein for studying amyloidosis. This work explores the potential of employing Lysozyme encapsulated gold nanoclusters (Ly-AuNCs) to study the protein’s aggregation. The fluorescence emission properties of Ly-AuNCs were studied in the presence of increasing concentrations of native lysozyme and as a function of pH, of relevance in macromolecular crowding and inflammation-triggered aggregation. AuNC fluorescence was observed to both redshift and increase in intensity as pH is increased or when native lysozyme is added to a solution of Ly-AuNCs at pH 3. The long (μs) fluorescence lifetime component of AuNC emission was observed to decrease under both conditions. Interestingly it was found via Time Resolved Emission Spectra (TRES) that both AuNC fluorescence components increase in intensity and redshift with increasing pH while only the long lifetime component of AuNC was observed to change when adding native lysozyme to solution; indicating that the underlying mechanisms for the changes observed are fundamentally different for each case. It is possible that the sensitivity of Ly-AuNCs to native lysozyme concentration could be utilized to study early stage aggregation.

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