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The Interactions Between Highly De-N-acetylated Chitosans And Lysozyme From Chicken Egg White Studied By 1H-NMR Spectroscopy.

A. Kristiansen, K. M. Vårum, H. Grasdalen
Published 1998 · Chemistry, Medicine

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We have investigated the binding interactions between highly de-N-acetylated chitosans and lysozyme from chicken egg white by one-dimensional and two-dimensional 1H-NMR spectroscopy. A fully de-N-acetylated chitosan (fraction of N-acetylated units, F < 0.001) induced no observable changes in the 1H chemical shifts of lysozyme. However, a chitosan with F(A) = 0.04, where the N-acetylated units are predominantly surrounded by de-N-acetylated units (a monoacetylated sequence), induced significant shifts of several lysozyme resonances, demonstrating a specific interaction between lysozyme and de-N-acetylated units in the chitosan. The interaction between the two positively charged molecules increased with increasing ionic strength, as expected. The dissociation constant (Kd) between lysozyme and the monoacetylated sequence was strongly dependent on pH* (pH measured in D2O), with Kd = 0.02+/-0.01 mM at pH* 6.0, Kd = 0.11+/-0.02 mM at pH* 4.5, and Kd approximately 2 mM at pH* 3, suggesting that electrostatic forces contribute to the observed binding. The complex was strikingly stable, with bound lifetimes in the range of 10-25 ms at pH* 4.5 and 328-300 K. Most lysozyme resonances that were affected by the binding were assigned, and we suggest that the monoacetylated chitosan sequence binds to the active site cleft of lysozyme with the N-acetylated unit in subsite C. Assuming this binding mode, we have discussed the contributions in energetic terms from individual subsites of lysozyme towards binding of N-acetylated and de-N-acetylated units.



This paper is referenced by
10.1271/bbb.65.1766
Binding of a Highly De-N-acetylated Chitosan to Japanese Pheasan Lysozyme as Measured by 1H-NMR Spectroscopy
T. Fukamizo (2001)
10.1016/S0008-6215(02)00334-8
Preparation and characterisation of chitosans with oligosaccharide branches.
K. Tømmeraas (2002)
Effects of chitosan on selected production characteristics and hatching success of the Pharaoh quail
Z. Tarasewicz (2003)
10.1271/bbb.70694
The Role of Arg114 at Subsites E and F in Reactions Catalyzed by Hen Egg-White Lysozyme
S. Kawamura (2008)
10.1107/S0909049505011647
Protein nanocrystallography: growth mechanism and atomic structure of crystals induced by nanotemplates.
E. Pechkova (2005)
10.3934/MATERSCI.2015.4.497
Degradation properties and metabolic activity of alginate and chitosan polyelectrolytes for drug delivery and tissue engineering applications
V. Guarino (2015)
Improved stem cell retention and mechanical stability in a chitosan-gelatin hydrogel
Christian J. Tormos (2016)
10.1016/J.CARRES.2006.11.016
Limitations of pH-potentiometric titration for the determination of the degree of deacetylation of chitosan.
N. Balázs (2007)
10.1016/B978-0-08-100228-5.00005-5
Chitosan for cardiac tissue engineering and regeneration
Christian J. Tormos (2017)
10.1016/S0928-0987(99)00032-9
Chitosans as absorption enhancers of poorly absorbable drugs. 3: Influence of mucus on absorption enhancement.
N. G. Schipper (1999)
Binding of a Highly De-IV-acetylated Lysozyme as Measured by iH-NMRChitosan to SpectroscopyJapanese Pheasan
T. Fukamizo (2018)
10.1111/j.1742-4658.2004.04495.x
Degradation of chitosans with chitinase B from Serratia marcescens
Audun Sørbotten (2005)
10.1016/j.carbpol.2015.05.077
NaOH treatment of chitosan films: Impact on macromolecular structure and film properties.
E. Takara (2015)
10.1134/S1061933X09020185
Properties of carrageenan gels with immobilized lysozyme
G. Yampol’skaya (2009)
10.1016/J.CARBPOL.2005.04.006
Optimal routine conditions for the determination of the degree of acetylation of chitosan by 1H-NMR
E. Fernandez-Megia (2005)
10.1021/acs.biomac.6b00547
Cellobiohydrolases Produce Different Oligosaccharides from Chitosan.
Gregor Tegl (2016)
10.1016/S0304-4165(98)00063-4
Quantitative studies of the non-productive binding of lysozyme to partially N-acetylated chitosans. Binding of large ligands to a one-dimensional binary lattice studied by a modified McGhee and von Hippel model.
A. Kristiansen (1998)
10.1016/J.MOLSTRUC.2008.10.058
A 1H NMR spectroscopic study on the tryptophan residues of lysozyme included by glucosyl-β-cyclodextrin
T. Yamamoto (2009)
10.1007/s00604-017-2481-z
A printed SWCNT electrode modified with polycatechol and lysozyme for capacitive detection of α-lactalbumin
Amal Raouafi (2017)
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