79. Su ZF, Jiang YX, Velazquez-Manzanares M, Leitch JJ, Kycia AH, Lipkowski J (2013)
Electrochemical and PM-IRRAS studies of floating lipid bilayers assembled at the Au(111)
electrode pre-modified with a hydrophilic monolayer. J Electroanal Chem 688:76–85
80. Lindstrom AB, Strynar MJ, Libelo EL (2011) Polyfluorinated compounds: past, present, and
future. Environ Sci Technol 45:7954–7961
81. Khandelia H, Ipsen JH, Mouritsen OG (2008) The impact of peptides on lipid membranes.
Biochim Biophys Acta 1778:1528–1536
82. Mouritsen OG, Bloom M (1993) Models of lipid-protein interactions in membranes. Annu
Rev Biophys Biomol Struct 22:145–171
83. Sackmann E (1984) Physical basis of trigger processes and membrane structures. In: Chapman
D (ed) Biological membranes, vol 5. Academic, New York, pp 105–143
84. Fang Y, Hong Y, Webb B, Lahiri J (2006) Applications of biomembranes in drug discovery.
MRS Bull 31:541–545
85. Tatulian SA (2013) Structural characterization of membrane proteins and peptides by FTIR
and ATR-FTIR spectroscopy. In: Kleinschmidt JH (ed) Lipid-protein interactions. Methods
and protocols, Methods in molecular biology, vol 974. Springer, New York, pp 177–218
86. Barth A (2007) Infrared spectroscopy of proteins. Biochim Biophys Acta 1767:1073–1101
87. Barth A, Zscherp C (2002) What vibrations tell us about proteins. Q Rev Biophys 35:369–430
88. Byler DM, Susi H (1986) Examination of the secondary structure of proteins by deconvolved
FTIR spectra. Biopolymers 25:469–487
89. Susi H, Byler DM (1987) Fourier transform infrared study of proteins with parallel β-chains.
Arch Biochem Biophys 258:465–469
90. Lee DC, Haris PI, Chapman D, Mitchell RC (1990) Determination of protein secondary
structure using factor analysis of infrared spectra. Biochemistry 29:9185–9193
91. Dousseau F, Pezolet M (1990) Determination of the secondary structure content of proteins in
aqueous solutions from their amide I and amide III infrared bands. Comparison between
classical and partial least-squares methods. Biochemistry 29:8771–8779
92. Kalnin NN, Baikalov IA, Venyaminov SY (1990) Quantitative IR spectrophotometry of
peptide compounds in water (H2O) solutions. III. Estimation of the protein secondary structure. Biopolymers 30:1273–1280
93. Pribic R, van Stokkum IHM, Chapman D, Haris PI, Blomendal M (1993) Protein secondary
structure from Fourier transform infrared and/or circular dichroism spectra. Anal Biochem
214:366–378
94. Abbasi F, Su ZF, Alvarez-Malmagro J, Leitch JJ, Lipkowski J (2019) Effects of amiloride, an
ion channel blocker, on alamethicin pore formation in negatively charged, gold-supported,
phospholipid bilayers: a molecular view. Langmuir 35:5060–5068
95. Su FZ, Shodiev M, Leitch JJ, Abbasi F, Lipkowski J (2018) In situ electrochemical and
PM-IRRAS studies of alamethicin ion channel formation in model phospholipid bilayers. J
Electroanal Chem 819:251–259
96. Su ZF, Leitch JJ, Abbasi F, Fargher RJ, Schwan AL (2018) EIS and PM-IRRAS studies of
alamethicin ion channels in a tethered lipid bilayer. J Electroanal Chem 812:213–220
97. Fox RO Jr, Richards FM (1982) A voltage-gated ion channel model inferred from the crystal
structure of alamethicin at 1.5 A resolution. Nature 300:325–330
98. Su ZF, Shodiev M, Leitch JJ, Abbasi F, Lipkowski J (2018) Role of transmembrane potential
and defects on the permeabilization of lipid bilayers by alamethicin, an ion-channel-forming
peptide. Langmuir 34:6249–6260
99. Marsh D, Müller M, Schmitt FJ (2000) Orientation of the infrared transition moments for an
α-helix. Biophys J 78:2499–2510
100. Miyazawa T, Blout ER (1961) The infrared spectra of polypeptides in various conformations:
amide I and II bands. J Am Chem Soc 83:712–719
101. Su ZF, Ho D, Merrill AR, Lipkowski J (2019) In situ electrochemical and PM-IRRAS studies
of colicin E1 ion channels in the floating bilayer lipid membrane. Langmuir 35:8452–8459
94
3 In Situ PM IRRAS Studies of Redox-Inactive Molecular Films Adsorbed on. . .
Electrochemical and PM-IRRAS studies of floating lipid bilayers assembled at the Au(111)
electrode pre-modified with a hydrophilic monolayer. J Electroanal Chem 688:76–85
80. Lindstrom AB, Strynar MJ, Libelo EL (2011) Polyfluorinated compounds: past, present, and
future. Environ Sci Technol 45:7954–7961
81. Khandelia H, Ipsen JH, Mouritsen OG (2008) The impact of peptides on lipid membranes.
Biochim Biophys Acta 1778:1528–1536
82. Mouritsen OG, Bloom M (1993) Models of lipid-protein interactions in membranes. Annu
Rev Biophys Biomol Struct 22:145–171
83. Sackmann E (1984) Physical basis of trigger processes and membrane structures. In: Chapman
D (ed) Biological membranes, vol 5. Academic, New York, pp 105–143
84. Fang Y, Hong Y, Webb B, Lahiri J (2006) Applications of biomembranes in drug discovery.
MRS Bull 31:541–545
85. Tatulian SA (2013) Structural characterization of membrane proteins and peptides by FTIR
and ATR-FTIR spectroscopy. In: Kleinschmidt JH (ed) Lipid-protein interactions. Methods
and protocols, Methods in molecular biology, vol 974. Springer, New York, pp 177–218
86. Barth A (2007) Infrared spectroscopy of proteins. Biochim Biophys Acta 1767:1073–1101
87. Barth A, Zscherp C (2002) What vibrations tell us about proteins. Q Rev Biophys 35:369–430
88. Byler DM, Susi H (1986) Examination of the secondary structure of proteins by deconvolved
FTIR spectra. Biopolymers 25:469–487
89. Susi H, Byler DM (1987) Fourier transform infrared study of proteins with parallel β-chains.
Arch Biochem Biophys 258:465–469
90. Lee DC, Haris PI, Chapman D, Mitchell RC (1990) Determination of protein secondary
structure using factor analysis of infrared spectra. Biochemistry 29:9185–9193
91. Dousseau F, Pezolet M (1990) Determination of the secondary structure content of proteins in
aqueous solutions from their amide I and amide III infrared bands. Comparison between
classical and partial least-squares methods. Biochemistry 29:8771–8779
92. Kalnin NN, Baikalov IA, Venyaminov SY (1990) Quantitative IR spectrophotometry of
peptide compounds in water (H2O) solutions. III. Estimation of the protein secondary structure. Biopolymers 30:1273–1280
93. Pribic R, van Stokkum IHM, Chapman D, Haris PI, Blomendal M (1993) Protein secondary
structure from Fourier transform infrared and/or circular dichroism spectra. Anal Biochem
214:366–378
94. Abbasi F, Su ZF, Alvarez-Malmagro J, Leitch JJ, Lipkowski J (2019) Effects of amiloride, an
ion channel blocker, on alamethicin pore formation in negatively charged, gold-supported,
phospholipid bilayers: a molecular view. Langmuir 35:5060–5068
95. Su FZ, Shodiev M, Leitch JJ, Abbasi F, Lipkowski J (2018) In situ electrochemical and
PM-IRRAS studies of alamethicin ion channel formation in model phospholipid bilayers. J
Electroanal Chem 819:251–259
96. Su ZF, Leitch JJ, Abbasi F, Fargher RJ, Schwan AL (2018) EIS and PM-IRRAS studies of
alamethicin ion channels in a tethered lipid bilayer. J Electroanal Chem 812:213–220
97. Fox RO Jr, Richards FM (1982) A voltage-gated ion channel model inferred from the crystal
structure of alamethicin at 1.5 A resolution. Nature 300:325–330
98. Su ZF, Shodiev M, Leitch JJ, Abbasi F, Lipkowski J (2018) Role of transmembrane potential
and defects on the permeabilization of lipid bilayers by alamethicin, an ion-channel-forming
peptide. Langmuir 34:6249–6260
99. Marsh D, Müller M, Schmitt FJ (2000) Orientation of the infrared transition moments for an
α-helix. Biophys J 78:2499–2510
100. Miyazawa T, Blout ER (1961) The infrared spectra of polypeptides in various conformations:
amide I and II bands. J Am Chem Soc 83:712–719
101. Su ZF, Ho D, Merrill AR, Lipkowski J (2019) In situ electrochemical and PM-IRRAS studies
of colicin E1 ion channels in the floating bilayer lipid membrane. Langmuir 35:8452–8459
94
3 In Situ PM IRRAS Studies of Redox-Inactive Molecular Films Adsorbed on. . .