Trypsin and trypsin inhibitor bind PAMAM nanoparticles: Effect of hydrophobicity on protein–polymer conjugation

Trypsin and trypsin inhibitor bind PAMAM nanoparticles: Effect of hydrophobicity on... 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 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Colloid and Interface Science Elsevier

Trypsin and trypsin inhibitor bind PAMAM nanoparticles: Effect of hydrophobicity on protein–polymer conjugation

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Publisher
Elsevier
Copyright
Copyright © 2015 Elsevier Inc.
ISSN
0021-9797
eISSN
1095-7103
D.O.I.
10.1016/j.jcis.2015.09.048
Publisher site
See Article on Publisher Site

Abstract

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

Journal of Colloid and Interface ScienceElsevier

Published: Jan 1, 2016

References

  • Biomacromolecules
    Mansson, R.; Frenning, G.; Malmsten, M.

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