Fluorescence-Based Approaches for Quantitative Assessment of Protein Carbonylation, Protein Disulfides, and Protein Conformation in Biological Tissues.

Asish R Chaudhuri, Rochelle Wei, Arunabh Bhattacharya, Ryan Hamilton

Journal: Methods in molecular biology (Clifton, N.J.) 2016;1343():155-73

PMID: 26420716

Abstract

Protein oxidation and misfolding have been considered as key players for progression of aging and etiology of various pathological conditions. However, few attempts have been made to develop sensitive and reproducible assays to quantify the changes in protein oxidation and alteration in structure. Here we describe three distinct fluorescence-based assays to quantify changes in protein oxidation, namely carbonylation and disulfides and alteration in protein surface hydrophobicity as a reporter for protein conformation. These techniques will provide investigators the opportunity to address important biological questions in their experimental models.

Address: UT Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX, 75390, USA. [email protected].; Barshop Institute for Longevity and Aging Studies, University of Texas Health Science Center at San Antonio, 15355 Lambda Drive, San Antonio, TX, 78245, USA. [email protected].; Departments of Biochemistry, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX, 78229, USA. [email protected].; South Texas Veterans Health Care System, San Antonio, TX, 78229, USA. [email protected].; Barshop Institute for Longevity and Aging Studies, University of Texas Health Science Center at San Antonio, 15355 Lambda Drive, San Antonio, TX, 78245, USA.; Cellular and Structural Biology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX, 78229, USA.

DOI: 10.1007/978-1-4939-2963-4_13

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https://doi.org/10.1007/978-1-4939-2963-4_13

MeSH Terms: Disulfides, Fluorescence, Optical Imaging, Oxidation-Reduction, Oxidative Stress, Protein Carbonylation, Protein Conformation, Proteins