Analytica Chimica Acta, accepted, 07/07/2015. This is the accepted version without proofing
corrections. DOI: 10.1016/j.aca.2015.06.011
.
Page 17 of 26
[36]
J.C.G.E. da Silva, R. Tauler, Multivariate curve resolution of synchronous fluorescence
spectra matrices of fulvic acids obtained as a function of pH, Appl. Spectrosc., 60 (2006) 1315-1321.
[37]
A. de Juan, R. Tauler, Multivariate curve resolution (MCR) from 2000: Progress in concepts
and applications, Crit. Rev. Anal. Chem., 36 (2006) 163-176.
[38]
R. Bro, PARAFAC. Tutorial and applications, Chemometr. Intell. Lab. Syst., 38 (1997) 149171.
[39]
C. Andersen, R. Bro, Practical aspects of PARAFAC modeling of fluorescence excitationemission data, J. Chemometr., 17 (2003) 200-215.
[40]
H. Chen, J.E. Kenny, Application of PARAFAC to a two-component system exhibiting
Fluorescence Resonance Energy Transfer: from theoretical prediction to experimental validation,
Analyst, 137 (2012) 153-162.
[41]
R.C. Groza, A. Calvet, A.G. Ryder, A fluorescence anisotropy method for measuring protein
concentration in complex cell culture media, Anal Chim Acta, 821 (2014) 54-61.
[42]
Y.J. Liu, H.L. Wu, C. Kang, H.W. Gu, J.F. Nie, S.S. Li, Z.Y. Su, R.Q. Yu, Four-way Selfweighted Alternating Normalized Residue Fitting Algorithm with Application for the Analysis of
Serotonin in Human Plasma, Analytical Sciences, 28 (2012) 1097-1104.
[43]
A.C. Olivieri, J.A. Arancibia, A.M. de la Pena, I. Duran-Meras, A.E. Mansilla, Second-order
advantage achieved with four-way fluorescence excitation-emission-kinetic data processed by parallel
factor analysis and trilinear least-squares. Determination of methotrexate and leucovorin in human
urine, Anal. Chem., 76 (2004) 5657-5666.
[44]
C.J. Xu, Y.Z. Liang, Y. Li, Y.P. Du, Chemical rank estimation by noise perturbation in
functional principal component analysis, Analyst, 128 (2003) 75-81.
[45]
Y. Hu, B.Y. Li, H. Sato, I. Noda, Y. Ozaki, Noise perturbation in functional principal
component analysis filtering for two-dimensional correlation spectroscopy: Its theory and application
to infrared spectra of a poly(3-hydroxybutyrate) thin film, Journal of Physical Chemistry A, 110
(2006) 11279-11290.
[46]
Y. Wei, C. Dong, D. Liu, S. Shuang, C.W. Huie, Enantioselective quenching of roomtemperature phosphorescence lifetimes of proteins: bovine and human serum albumins,
Biomacromolecules, 8 (2007) 761-764.
[47]
S. Tabassum, W.M. Al-Asbahy, M. Afzal, F. Arjmand, R.H. Khan, Interaction and photoinduced cleavage studies of a copper based chemotherapeutic drug with human serum albumin:
spectroscopic and molecular docking study, Molecular bioSystems, 8 (2012) 2424-2433.
[48]
Y. Moriyama, K. Takeda, Re-formation of the helical structure of human serum albumin by
the addition of small amounts of sodium dodecyl sulfate after the disruption of the structure by urea.
A comparison with bovine serum albumin, Langmuir, 15 (1999) 2003-2008.
[49]
Y. Moriyama, K. Takeda, Protective effects of small amounts of bis(2ethylhexyl)sulfosuccinate on the helical structures of human and bovine serum albumins in their
thermal denaturations, Langmuir, 21 (2005) 5524-5528.
[50]
M. Rezaei-Tavirani, S.H. Moghaddamnia, B. Ranjbar, M. Amani, S.A. Marashi,
Conformational study of human serum albumin in pre-denaturation temperatures by differential
scanning calorimetry, circular dichroism and UV spectroscopy, J. Biochem. Mol. Biol., 39 (2006)
530-536.
[51]
M. Dockal, D.C. Carter, F. Ruker, Conformational transitions of the three recombinant
domains of human serum albumin depending on pH, Journal of Biological Chemistry, 275 (2000)
3042-3050.
[52]
J. Juarez, P. Taboada, V. Mosquera, Existence of Different Structural Intermediates on the
Fibrillation Pathway of Human Serum Albumin, Biophys. J., 96 (2009) 2353-2370.
corrections. DOI: 10.1016/j.aca.2015.06.011
.
Page 17 of 26
[36]
J.C.G.E. da Silva, R. Tauler, Multivariate curve resolution of synchronous fluorescence
spectra matrices of fulvic acids obtained as a function of pH, Appl. Spectrosc., 60 (2006) 1315-1321.
[37]
A. de Juan, R. Tauler, Multivariate curve resolution (MCR) from 2000: Progress in concepts
and applications, Crit. Rev. Anal. Chem., 36 (2006) 163-176.
[38]
R. Bro, PARAFAC. Tutorial and applications, Chemometr. Intell. Lab. Syst., 38 (1997) 149171.
[39]
C. Andersen, R. Bro, Practical aspects of PARAFAC modeling of fluorescence excitationemission data, J. Chemometr., 17 (2003) 200-215.
[40]
H. Chen, J.E. Kenny, Application of PARAFAC to a two-component system exhibiting
Fluorescence Resonance Energy Transfer: from theoretical prediction to experimental validation,
Analyst, 137 (2012) 153-162.
[41]
R.C. Groza, A. Calvet, A.G. Ryder, A fluorescence anisotropy method for measuring protein
concentration in complex cell culture media, Anal Chim Acta, 821 (2014) 54-61.
[42]
Y.J. Liu, H.L. Wu, C. Kang, H.W. Gu, J.F. Nie, S.S. Li, Z.Y. Su, R.Q. Yu, Four-way Selfweighted Alternating Normalized Residue Fitting Algorithm with Application for the Analysis of
Serotonin in Human Plasma, Analytical Sciences, 28 (2012) 1097-1104.
[43]
A.C. Olivieri, J.A. Arancibia, A.M. de la Pena, I. Duran-Meras, A.E. Mansilla, Second-order
advantage achieved with four-way fluorescence excitation-emission-kinetic data processed by parallel
factor analysis and trilinear least-squares. Determination of methotrexate and leucovorin in human
urine, Anal. Chem., 76 (2004) 5657-5666.
[44]
C.J. Xu, Y.Z. Liang, Y. Li, Y.P. Du, Chemical rank estimation by noise perturbation in
functional principal component analysis, Analyst, 128 (2003) 75-81.
[45]
Y. Hu, B.Y. Li, H. Sato, I. Noda, Y. Ozaki, Noise perturbation in functional principal
component analysis filtering for two-dimensional correlation spectroscopy: Its theory and application
to infrared spectra of a poly(3-hydroxybutyrate) thin film, Journal of Physical Chemistry A, 110
(2006) 11279-11290.
[46]
Y. Wei, C. Dong, D. Liu, S. Shuang, C.W. Huie, Enantioselective quenching of roomtemperature phosphorescence lifetimes of proteins: bovine and human serum albumins,
Biomacromolecules, 8 (2007) 761-764.
[47]
S. Tabassum, W.M. Al-Asbahy, M. Afzal, F. Arjmand, R.H. Khan, Interaction and photoinduced cleavage studies of a copper based chemotherapeutic drug with human serum albumin:
spectroscopic and molecular docking study, Molecular bioSystems, 8 (2012) 2424-2433.
[48]
Y. Moriyama, K. Takeda, Re-formation of the helical structure of human serum albumin by
the addition of small amounts of sodium dodecyl sulfate after the disruption of the structure by urea.
A comparison with bovine serum albumin, Langmuir, 15 (1999) 2003-2008.
[49]
Y. Moriyama, K. Takeda, Protective effects of small amounts of bis(2ethylhexyl)sulfosuccinate on the helical structures of human and bovine serum albumins in their
thermal denaturations, Langmuir, 21 (2005) 5524-5528.
[50]
M. Rezaei-Tavirani, S.H. Moghaddamnia, B. Ranjbar, M. Amani, S.A. Marashi,
Conformational study of human serum albumin in pre-denaturation temperatures by differential
scanning calorimetry, circular dichroism and UV spectroscopy, J. Biochem. Mol. Biol., 39 (2006)
530-536.
[51]
M. Dockal, D.C. Carter, F. Ruker, Conformational transitions of the three recombinant
domains of human serum albumin depending on pH, Journal of Biological Chemistry, 275 (2000)
3042-3050.
[52]
J. Juarez, P. Taboada, V. Mosquera, Existence of Different Structural Intermediates on the
Fibrillation Pathway of Human Serum Albumin, Biophys. J., 96 (2009) 2353-2370.