Monitoring the assembly and aggregation of polypeptide materials by time-resolved emission spectra

Abeer Alghamdi; Li Hung C. Chung; Olaf J. Rolinski

doi:10.1007/978-1-0716-0928-6_11

Monitoring the assembly and aggregation of polypeptide materials by time-resolved emission spectra

Abeer Alghamdi, Li Hung C. Chung, Olaf J. Rolinski^*

^*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

Polypeptide assembly and aggregation are the common forms of its physiological and pathological activity, and monitoring them on a molecular level is critical for resolving numerous medical (e.g., onset of neurodegenerative diseases) or biological problems. Sensitivity of the intrinsic fluorescence of protein to its assembly, aggregation, or complexation offers a noninvasive methodology for identifying and determining different stages of these processes. In this protocol, we present the approach based on the time-resolved emission spectra (TRES), which reveals the number of fluorescent residues, the presence of dielectric relaxation, and the changes in fluorescence kinetics during aggregation.

Original language	English
Title of host publication	Methods in Molecular Biology
Editors	Maxim G. Ryadnov
Place of Publication	New York, NY
Pages	167-177
Number of pages	11
ISBN (Electronic)	9781071609286
DOIs	https://doi.org/10.1007/978-1-0716-0928-6_11
Publication status	Published - 2021

Publication series

Name	Methods in Molecular Biology
Volume	2208
ISSN (Print)	1064-3745
ISSN (Electronic)	1940-6029

Funding

We acknowledge funding for studentships from the UK?s Engineering and Physical Sciences Research Council (industry case award) to C. Chung and from the Princess Nourah bint Abdulrahman University to A. Alghamdi.

Keywords

dielectric relaxation
fluorescence intensity decay
intrinsic fluorescence
protein assembly and aggregation
time-resolved emission spectra

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10.1007/978-1-0716-0928-6_11

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AB - Polypeptide assembly and aggregation are the common forms of its physiological and pathological activity, and monitoring them on a molecular level is critical for resolving numerous medical (e.g., onset of neurodegenerative diseases) or biological problems. Sensitivity of the intrinsic fluorescence of protein to its assembly, aggregation, or complexation offers a noninvasive methodology for identifying and determining different stages of these processes. In this protocol, we present the approach based on the time-resolved emission spectra (TRES), which reveals the number of fluorescent residues, the presence of dielectric relaxation, and the changes in fluorescence kinetics during aggregation.

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KW - fluorescence intensity decay

KW - intrinsic fluorescence

KW - protein assembly and aggregation

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A2 - Ryadnov, Maxim G.

CY - New York, NY

ER -

Monitoring the assembly and aggregation of polypeptide materials by time-resolved emission spectra

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