Identification of a molten globule like state in HC-N Fragment of botulinum neurotoxin A: Shedding light on the poorly-known features of a conserved sub-domain

Protein and Peptide Letters

Volumn 16, Issue 6, 2009, Pages 660-663

  Hasani, Leila ^a   Ranjbar, Bijan ^a   Tavallaie, Mahmood ^b   Sadeghizadeh, Majid ^a  

^a TARBIAT MODARES UNIVERSITY   (Iran)

^b PASTEUR INSTITUTE OF IRAN   (Iran)

Author keywords

Botulinum neurotoxin A; Circular dichroism; Fluorescence spectroscopy; HC N; Molten globule like state

Indexed keywords

BOTULINUM TOXIN A; DODECYL SULFATE SODIUM; GUANIDINE; PEPTIDE FRAGMENT;

ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; SPECTROFLUOROMETRY;

BOTULINUM TOXIN TYPE A; CIRCULAR DICHROISM; GUANIDINE; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SODIUM DODECYL SULFATE; SPECTROMETRY, FLUORESCENCE;

EID: 67650162527     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609788490131     Document Type: Article

References (16)

1. Schiavo, G.; Matteoli, M.; Montecucco, C. Neurotoxins affecting neuroexocytosis. Physiol. Rev., 2000, 2, 717-765.
2. Lacky, D. B.; Tepp, W.; Cohen, A.; Dasgupta, C. B. R.; Stevens, R. C. Crystal structure of Botulinum neurotoxin type A and implications for toxicity. Nature Struct. Biol., 1998, 5, 898-902.
3. Turton, K.; Chaddock, J. A.; Ravi Acharya, K. Botulinum and Tetanus neurotoxins: Structure, function and therapeutic utility. Trends Biochem. Sci., 2002, 11, 552-558.
4. Tavallaie, M.; Chenal, A.; Gillet, D.; Pereira, Y.; Manich, M.; Gilbert, M.; Raffestin, S.; Popoff, M. R.; Maraud, J. C. Interaction between the two subdomains of the C-terminal part of the Botulinumneurotoxin A is essential for the generation of protective antibodies. FEBS Lett., 2004, 572, 299-306.
5. Maksymowych, A. B.; Simpson, L. L. Structural Features of the Botulinum neurotoxin molecule that govern binding and transcytosis across polarized human intestinal epithelial cells. J. Pharmacol. Exp. Ther., 2004, 310, 633-640.
6. Fujinaga, Y. Transport of Bacterial Toxins into Target Cells: Pathways followed by Cholera Toxin and Botulinum Progenitor Toxin. J. Biochem., 2006, 140, 155-160.
7. Schellman, J.A. Fifty years of solvent denaturation. Biophys. Chem., 2002, 96, 91-101.
8. Bhowmick, R.; Jagannadham, M. V. SDS-induced conformational transitions of eravatamin B: Evidence of greater stability of -rich domain compared to -rich domain of the SDS derived state. Colloids Surfaces, 2003, 32, 223-234.
9. Reynolds, J.A.; Tanford, C. Binding of Dodecyl sulfate to proteins at high binding ratios. Possible implications for the state of proteins in biological membranes. PNAS, 1970, 66, 1002-1007.
10. Hosseinkhani, S.; Ranjbar, B.; Naderi-Manesh, H.; Nemat-Gorgani, M. Chemical modification of glucose oxidase: possible formation of molten globule-like intermediate structure. FEBS Lett., 2004,561, 213-216.
11. Srimathi, T.; Kumar, T.K.S.; Chi, Y.; Chiu, I.; Yu, C. Characterization of the structure and dynamics of Near-native equilibrium intermediate in the unfolding pathway of an all -barrel protein. J. Biol. Chem., 2002, 277, 47507- 47516.
12. Protasevich, I.; Ranjbar, B.; Lobachov, V.; Markov, A.; Gilli, D.; Briand, D.; Lafitte, J.; Haiech, R. Conformation and thermal denaturation of Apocalmodulin: Role of electrostatic mutations. Biochemistry,1997, 36, 2017-2024.
13. Hassani, L.; Ranjbar, B.; Khajeh, K.; Naderi-Manesh, H.; Naderi- Manesh, M.; Sadeghi. M. Horseradish peroxidase thermostabilization: The combinatorial effects of the surface modification and the polyols. Enz. Microb. Technol., 2006, 38, 118-125.
14. Kelly, S. M.; Price, N. C. The use of circular dichroism in the investigation protein structure and function. Curr. Protein Pept. Sci., 2000, 1, 349-384.
15. Chen, Y. H.; Yang, J. T.; Martinez, H. M. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry, 1972, 11, 4120-4131.
16. Royer C. A. Approaches to teaching fluorescence spectroscopy. Biophys. J., 1995, 68, 1191-1195.