Chitosan nanoparticles conjugate with trypsin and trypsin inhibitor

[Display omitted] •The conjugation of chitosan nanoparticles with trypsin and trypsin inhibitor is studied here.•Chitosan nanoparticles bind trypsin and trypsin inhibitor via hydrophilic, hydrophobic, H-bonding and van der Waals interactions.•As chitosan size increases the stability of chitosan-prot...

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Bibliographic Details
Published inCarbohydrate polymers Vol. 144; pp. 346 - 352
Main Authors Chanphai, P., Tajmir-Riahi, H.A.
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 25.06.2016
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Summary:[Display omitted] •The conjugation of chitosan nanoparticles with trypsin and trypsin inhibitor is studied here.•Chitosan nanoparticles bind trypsin and trypsin inhibitor via hydrophilic, hydrophobic, H-bonding and van der Waals interactions.•As chitosan size increases the stability of chitosan-protein conjugate increases.•Trypsin inhibitor forms more stable chitosan conjugates than trypsin.•Chitosan interaction alters protein secondary structure for both trypsin and trypsin inhibitor causing a partial protein destabilization. Chitosan-protein conjugates are widely used in therapeutic drug delivery. We report the bindings of chitosan nanoparticles with trypsin (try) and trypsin inhibitor (tryi), using thermodynamic analysis and multiple spectroscopic methods. Thermodynamic parameters ΔS, ΔH and ΔG showed chitosan-protein bindings occur mainly via H-bonding and van der Waals contacts with trypsin inhibitor forming more stable conjugate than trypsin. As chitosan size increased more stable polymer-protein conjugate was formed. Chitosan complexation induces more perturbations of trypsin inhibitor structure than trypsin with reduction of protein alpha-helix and major increase of random structure. The negative value of ΔG indicates spontaneous protein-chitosan complexation at room temperature. Chitosan nanoparticles can be used to transport trypsin and trypsin inhibitor.
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ISSN:0144-8617
1879-1344
DOI:10.1016/j.carbpol.2016.02.066