Changes in Conformation of Human Neuronal Tau During Denaturation in Formaldehyde Solution

Authors: Chun-Lai Nie; Wei Zhang; Dai Zhang; Rong-Qiao He

Source: Protein and Peptide Letters, Volume 12, Number 1, January 2005 , pp. 75-78(4)

Publisher: Bentham Science Publishers

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Abstract:

Human neuronal tau was incubated in formaldehyde solution at low concentrations and the intensity of light scattering of tau-40 solution at 480 nm increased markedly. Then potassium iodide was used to quench the intrinsic fluorescence of tau. The fluorescent quenching constants decreased as formaldehyde concentrations increased. 8-anilino- 1-naphthalenesulfonic acid (ANS) binding assay showed that a putative hydrophobic core formed in tau polymers during incubation with formaldehyde. Native tau was hydrolyzed by immobilized earthworm fibrinolytic enzyme-II (EFE-II), producing a digested fragment (36-37 kDa). However, formaldehyde-treated tau could not be digested under the same conditions, suggesting that aggregated protein was relatively rigidly deposited.

Keywords: human neuronal tau; 8-anilino-1-naphthalenesulfonic acid; tau aggregation; denaturation; formaldehyde

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866053405931

Affiliations: 1: Institute of Biophysics, Chinese Academy of Sciences, Beijing University, Beijing.

Publication date: 2005-01-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.