pH-induced changes in β-casomorphin 7 structure studied by 1H nuclear magnetic resonance and Fourier-transform infrared spectroscopy
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Alderson, 2018, Propensity for cis-proline formation in unfolded proteins, ChemBioChem, 19, 10.1002/cbic.201700548
Asledottir, 2017, Identification of bioactive peptides and quantification of β-casomorphin-7 from bovine β-casein A1, A2 and I after ex vivo gastrointestinal digestion, International Dairy Journal, 71, 98, 10.1016/j.idairyj.2017.03.008
Barth, 2000, The infrared absorption of amino acid side chains, Progress in Biophysics and Molecular Biology, 74, 141, 10.1016/S0079-6107(00)00021-3
Basosi, 2001, cis–trans Isomerization of β-casomorphin peptides bound to copper (II): integration of EPR and NMR studies, Journal of the Chemical Society, Perkin Transactions, 2, 252, 10.1039/b004964f
Bax, 1985, MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy, Journal of Magnetic Resonance, 65, 355
Christl, 1972, Nuclear magnetic resonance spectroscopy. Carbon-13 chemical shifts of small peptides as a function of pH, Journal of the American Chemical Society, 94, 4565, 10.1021/ja00768a026
Cieślińska, 2007, Beta-casomorphin 7 in raw and hydrolyzed milk derived from cows of alternative β-casein genotypes, Milchwissenschaft, 62, 125
Daniloski, 2021, Health-related outcomes of genetic polymorphism of bovine β-casein variants: A systematic review of randomised controlled trials, Trends in Food Science & Technology, 111, 233, 10.1016/j.tifs.2021.02.073
De Noni, 2008, Release of β-casomorphins 5 and 7 during simulated gastro-intestinal digestion of bovine β-casein variants and milk-based infant formulas, Food Chemistry, 110, 897, 10.1016/j.foodchem.2008.02.077
Farahani, 2014, Proline N-oxides: Modulators of the 3D conformation of linear peptides through “NO-turns”, Organic and Biomolecular Chemistry, 12, 4479, 10.1039/c4ob00433g
Hernandez, 2009, Vibrational analysis of amino acids and short peptides in hydrated media. IV. Amino acids with hydrophobic side chains: l-Alanine, l-valine, and l-isoleucine, Journal of Physical Chemistry B, 113, 3169, 10.1021/jp809204d
Huppertz, 2013, Chemistry of the caseins, Vol. 1A, 135
Hwang, 1995, Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients, Journal of Magnetic Resonance, Series A, 112, 275, 10.1006/jmra.1995.1047
Jarmołowska, 2007, Serum activity of dipeptidyl peptidase IV (DPPIV; EC 3.4. 14.5) in breast-fed infants with symptoms of allergy, Peptides, 28, 678, 10.1016/j.peptides.2006.11.014
Jinsmaa, 1999, Enzymatic release of neocasomorphin and β-casomorphin from bovine β-casein, Peptides, 20, 957, 10.1016/S0196-9781(99)00088-1
Lambers, 2021, Processing affects beta-casomorphin peptide formation during simulated gastrointestinal digestion in both A1 and A2 milk, International Dairy Journal, 121, 105099, 10.1016/j.idairyj.2021.105099
Lin, 1985, Isomer-specific proteolysis of model substrates: Influence that the location of the proline residue exerts on cis trans specificity, Biochemistry, 24, 6533, 10.1021/bi00344a034
Marion, 1983, Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H–1H spin-spin coupling constants in proteins, Biochemical and Biophysical Research Communications, 113, 967, 10.1016/0006-291X(83)91093-8
Markoska, 2020, Unravelling conformational aspects of milk protein structure - Contributions from nuclear magnetic resonance studies, Foods, 9, 10.3390/foods9081128
Moorthi, 2014, Vibrational spectroscopic studies of isoleucine by quantum chemical calculations, Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 124, 365, 10.1016/j.saa.2014.01.067
Nguyen, 2021, Release of beta-casomorphins during in-vitro gastrointestinal digestion of reconstituted milk after heat treatment, LWT, 136, 10.1016/j.lwt.2020.110312
Nguyen, 2015, Formation and degradation of beta-casomorphins in dairy processing, Critical Reviews in Food Science and Nutrition, 55, 1955, 10.1080/10408398.2012.740102
Seavey, 1991, A relational database for sequence-specific protein NMR data, Journal of Biomolecular NMR, 1, 217, 10.1007/BF01875516
Shiga, 2010, The chemical shift of deprotonated water dimer: Ab initio path integral simulation, The Journal of Chemical Physics, 132, 10.1063/1.3354948
Tereshchenkova, 2016, Dipeptidyl peptidase 4 – An important digestive peptidase in Tenebrio molitor larvae, Insect Biochemistry and Molecular Biology, 76, 38, 10.1016/j.ibmb.2016.07.003
Thiruvengadam, 2021, β-Casomorphin: A complete health perspective, Food Chemistry, 337, 10.1016/j.foodchem.2020.127765
Vance, 1997, Cleavage of the X–pro peptide bond by pepsin is specific for the trans isomer, Biochemistry, 36, 13232, 10.1021/bi970918b
Vien, 1991
Wedemeyer, 2002, Proline cis–trans isomerization and protein folding, Biochemistry, 41, 14637, 10.1021/bi020574b
Wüthrich, 1986, NMR with proteins and nucleic acids, Europhysics News, 17, 11, 10.1051/epn/19861701011