Analytica Chimica Acta, accepted, 07/07/2015. This is the accepted version without proofing
corrections. DOI: 10.1016/j.aca.2015.06.011
.
Page 15 of 26
RCG was supported by an ‘EMBARK Initiative’ Postgraduate Scholarship from the Irish Research
Council. We also thank Jeffrey Comerford and Ursula Tems of Agilent Technologies (Mulgrave
Victoria, Australia) for the loan of a fluorescence spectrometer.
References:
[1]
J.R. Lakowicz, Principles of Fluorescence Spectroscopy, Springer, New York, 2006.
[2]
I.B. Bekard, D.E. Dunstan, Tyrosine Autofluorescence as a Measure of Bovine Insulin
Fibrillation, Biophys. J., 97 (2009) 2521-2531.
[3]
D.M. Togashi, A.G. Ryder, D. O'Shaughnessy, Monitoring local unfolding of bovine serum
albumin during denaturation using steady-state and time-resolved fluorescence spectroscopy, Journal
of Fluorescence, 20 (2010) 441-452.
[4]
E. Lissi, C. Calderon, A. Campos, Evaluation of the Number of Binding Sites in Proteins
from their Intrinsic Fluorescence: Limitations and Pitfalls, Photochem. Photobiol., 89 (2013) 14131416.
[5]
K. Sagoo, R. Hirsch, P. Johnston, D. McLoskey, G. Hungerford, Pre-denaturing transitions in
human serum albumin probed time-resolved phosphorescence using, Spectroc. Acta Pt. A-Molec.
Biomolec. Spectr., 124 (2014) 611-617.
[6]
M.M. Khan, S. Muzammil, S. Tayyab, Role of salt bridge(s) in the binding and
photoconversion of bilirubin bound to high affinity site on human serum albumin, Biochim. Biophys.
Acta-Protein Struct. Molec. Enzym., 1479 (2000) 103-113.
[7]
J.K. Armstrong, R.B. Wenby, H.J. Meiselman, T.C. Fisher, The hydrodynamic radii of
macromolecules and their effect on red blood cell aggregation, Biophys. J., 87 (2004) 4259-4270.
[8]
N. Sattarahmady, A.A. Moosavi-Movahedi, F. Ahmad, G.H. Hakimelahi, M. Habibi-Rezaei,
A.A. Saboury, N. Sheibani, Formation of the molten globule-like state during prolonged glycation of
human serum albumin, Biochim. Biophys. Acta-Gen. Subj., 1770 (2007) 933-942.
[9]
R. Yadav, B. Sengupta, P. Sen, Conformational Fluctuation Dynamics of Domain I of Human
Serum Albumin in the Course of Chemically and Thermally Induced Unfolding Using Fluorescence
Correlation Spectroscopy, J. Phys. Chem. B, 118 (2014) 5428-5438.
[10]
U. Kragh-Hansen, V.T.G. Chuang, M. Otagiri, Practical aspects of the ligand-binding and
enzymatic properties of human serum albumin, Biol. Pharm. Bull., 25 (2002) 695-704.
[11]
J. Ghuman, P.A. Zunszain, I. Petitpas, A.A. Bhattacharya, M. Otagiri, S. Curry, Structural
basis of the drug-binding specificity of human serum albumin, J. Mol. Biol., 353 (2005) 38-52.
[12]
F. Kratz, Albumin as a drug carrier: Design of prodrugs, drug conjugates and nanoparticles,
Journal of Controlled Release, 132 (2008) 171-183.
[13]
S. Curry, H. Mandelkow, P. Brick, N. Franks, Crystal structure of human serum albumin
complexed with fatty acid reveals an asymmetric distribution of binding sites, Nat. Struct. Biol., 5
(1998) 827-835.
[14]
S. Sugio, A. Kashima, S. Mochizuki, M. Noda, K. Kobayashi, Crystal structure of human
serum albumin at 2.5 angstrom resolution, Protein Eng., 12 (1999) 439-446.
[15]
M.K. Santra, A. Banerjee, O. Rahaman, D. Panda, Unfolding pathways of human serum
albumin: Evidence for sequential unfolding and folding of its three domains, International Journal of
Biological Macromolecules, 37 (2005) 200-204.
[16]
O.K. Abou-Zied, O.I.K. Al-Shihi, Characterization of subdomain IIA binding site of human
serum albumin in its native, unfolded, and refolded states using small molecular probes, J. Am. Chem.
Soc., 130 (2008) 10793-10801.
corrections. DOI: 10.1016/j.aca.2015.06.011
.
Page 15 of 26
RCG was supported by an ‘EMBARK Initiative’ Postgraduate Scholarship from the Irish Research
Council. We also thank Jeffrey Comerford and Ursula Tems of Agilent Technologies (Mulgrave
Victoria, Australia) for the loan of a fluorescence spectrometer.
References:
[1]
J.R. Lakowicz, Principles of Fluorescence Spectroscopy, Springer, New York, 2006.
[2]
I.B. Bekard, D.E. Dunstan, Tyrosine Autofluorescence as a Measure of Bovine Insulin
Fibrillation, Biophys. J., 97 (2009) 2521-2531.
[3]
D.M. Togashi, A.G. Ryder, D. O'Shaughnessy, Monitoring local unfolding of bovine serum
albumin during denaturation using steady-state and time-resolved fluorescence spectroscopy, Journal
of Fluorescence, 20 (2010) 441-452.
[4]
E. Lissi, C. Calderon, A. Campos, Evaluation of the Number of Binding Sites in Proteins
from their Intrinsic Fluorescence: Limitations and Pitfalls, Photochem. Photobiol., 89 (2013) 14131416.
[5]
K. Sagoo, R. Hirsch, P. Johnston, D. McLoskey, G. Hungerford, Pre-denaturing transitions in
human serum albumin probed time-resolved phosphorescence using, Spectroc. Acta Pt. A-Molec.
Biomolec. Spectr., 124 (2014) 611-617.
[6]
M.M. Khan, S. Muzammil, S. Tayyab, Role of salt bridge(s) in the binding and
photoconversion of bilirubin bound to high affinity site on human serum albumin, Biochim. Biophys.
Acta-Protein Struct. Molec. Enzym., 1479 (2000) 103-113.
[7]
J.K. Armstrong, R.B. Wenby, H.J. Meiselman, T.C. Fisher, The hydrodynamic radii of
macromolecules and their effect on red blood cell aggregation, Biophys. J., 87 (2004) 4259-4270.
[8]
N. Sattarahmady, A.A. Moosavi-Movahedi, F. Ahmad, G.H. Hakimelahi, M. Habibi-Rezaei,
A.A. Saboury, N. Sheibani, Formation of the molten globule-like state during prolonged glycation of
human serum albumin, Biochim. Biophys. Acta-Gen. Subj., 1770 (2007) 933-942.
[9]
R. Yadav, B. Sengupta, P. Sen, Conformational Fluctuation Dynamics of Domain I of Human
Serum Albumin in the Course of Chemically and Thermally Induced Unfolding Using Fluorescence
Correlation Spectroscopy, J. Phys. Chem. B, 118 (2014) 5428-5438.
[10]
U. Kragh-Hansen, V.T.G. Chuang, M. Otagiri, Practical aspects of the ligand-binding and
enzymatic properties of human serum albumin, Biol. Pharm. Bull., 25 (2002) 695-704.
[11]
J. Ghuman, P.A. Zunszain, I. Petitpas, A.A. Bhattacharya, M. Otagiri, S. Curry, Structural
basis of the drug-binding specificity of human serum albumin, J. Mol. Biol., 353 (2005) 38-52.
[12]
F. Kratz, Albumin as a drug carrier: Design of prodrugs, drug conjugates and nanoparticles,
Journal of Controlled Release, 132 (2008) 171-183.
[13]
S. Curry, H. Mandelkow, P. Brick, N. Franks, Crystal structure of human serum albumin
complexed with fatty acid reveals an asymmetric distribution of binding sites, Nat. Struct. Biol., 5
(1998) 827-835.
[14]
S. Sugio, A. Kashima, S. Mochizuki, M. Noda, K. Kobayashi, Crystal structure of human
serum albumin at 2.5 angstrom resolution, Protein Eng., 12 (1999) 439-446.
[15]
M.K. Santra, A. Banerjee, O. Rahaman, D. Panda, Unfolding pathways of human serum
albumin: Evidence for sequential unfolding and folding of its three domains, International Journal of
Biological Macromolecules, 37 (2005) 200-204.
[16]
O.K. Abou-Zied, O.I.K. Al-Shihi, Characterization of subdomain IIA binding site of human
serum albumin in its native, unfolded, and refolded states using small molecular probes, J. Am. Chem.
Soc., 130 (2008) 10793-10801.