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Origin of Fluorescence Lifetimes in Human Serum Albumin. Studies on Native and Denatured Protein

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Abstract

Human serum albumin consists of a single polypeptide of 585 amino acid residues with 1 Trp residue. In the present work, we measured fluorescence lifetimes of the protein in both native and denatured states. The results indicate that Trp emission occurs with three lifetimes in both states. Lifetimes values and contribution to the global emission decay differ between the two states. Data are interpreted as the results of an emission occurring from three substructures of the tryptophan formed in the excited state. Two of these substructures are already present for the tryptophan free in solution. The third lifetime is the result of the interaction between the tryptophan residue and surrounding microenvironment. The populations of these substructures characterized by the pre-exponential parameters of the fluorescence lifetimes are dependent on the fluorophore microenvironment and on the global protein structure.

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Authors and Affiliations

  1. Laboratoire de Biophysique Moléculaire, Université des Sciences et Technologies de Lille, Bâtiment C6. 59655, Villeneuve d’Ascq Cédex, France

    Megdouda Amiri, Kristina Jankeje & Jihad René Albani

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  1. Megdouda Amiri
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  2. Kristina Jankeje
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  3. Jihad René Albani
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Correspondence to Jihad René Albani.

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Amiri, M., Jankeje, K. & Albani, J.R. Origin of Fluorescence Lifetimes in Human Serum Albumin. Studies on Native and Denatured Protein. J Fluoresc 20, 651–656 (2010). https://doi.org/10.1007/s10895-010-0597-1

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  • DOI: https://doi.org/10.1007/s10895-010-0597-1

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