Journal of Colloid and Interface Science 461 (2016) 419–424 Contents lists available at ScienceDirect Journal of Colloid and Interface Science journal homepage: www.elsevier.com/locate/jcis Trypsin and trypsin inhibitor bind PAMAM nanoparticles: Effect of hydrophobicity on protein–polymer conjugation P. Chanphai, H.A. Tajmir-Riahi Department of Chemistry-Biochemistry and Physics, University of Québec at Trois Rivières, C.P. 500, TR, Quebec G9A 5H7, Canada highl i ghts graphical a bstrac t Conjugations of trypsin and trypsin inhibitor with PAMAM-G4 nanoparticles are studied here. Protein–polymer interactions are via H-bonding and van der Waals contacts. Trypsin inhibitor forms stronger polymer adduct than trypsin. Hydrophobicity plays a role in polymer–protein conjugation. Polymer interaction alters protein conformation. article i nfo abstract Article history: Protein–polymer conjugates are widely used in therapeutic drug delivery. We report the bindings of Received 18 August 2015 trypsin (Try) and trypsin inhibitor (Tryi) with polyamidoamine (PAMAM-G4) dendrimer at physiological Revised 20 September 2015 conditions, using thermodynamic analysis, UV–Visible and Fourier transform infrared (FTIR) spectro- Accepted 21 September 2015 scopic methods. Thermodynamic parameters DS, DH and DG showed protein–PAMAM bindings occur Available online 25 September 2015 via H-bonding and van der Waals contacts with trypsin inhibitor forming more stable conjugate than trypsin. PAMAM complexation induces more
Journal of Colloid and Interface Science – Elsevier
Published: Jan 1, 2016
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