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Journal of Thermal Analysis and Calorimetry

, Volume 138, Issue 5, pp 3249–3256 | Cite as

Encapsulating properties of sulfobutylether-β-cyclodextrin toward a thrombin-derived antimicrobial peptide

  • Rosario Oliva
  • Filomena Battista
  • Serena Cozzolino
  • Eugenio Notomista
  • Roland Winter
  • Pompea Del Vecchio
  • Luigi PetracconeEmail author
Article
  • 73 Downloads

Abstract

The pharmacological application of antimicrobial peptides (AMPs) is seriously limited as they are not chemically and physically stable. Their encapsulation could represent a way to protect AMPs improving their pharmacological properties. In this study, the complex between the sulfobutylether-β-cyclodextrin (SBE-β-CD) and the antimicrobial peptide (P)GKY20 and its effect on a lipid bilayer have been characterized by a combination of calorimetric (ITC, DSC) and spectroscopic (fluorescence, Circular Dichroism) techniques. The results obtained indicate that the (P)GKY20 form a 1:1 inclusion complex with the anionic SBE-β-CD. Our ITC experiments revealed that the interaction process is entropically driven and that the enthalpy change only slightly contributes to the free energy change. Finally, differential scanning calorimetry data revealed that the peptide, even in the presence of SBE-β-CD, is still able to perturb the bacterial model membrane composed of DPPC/DPPG (8/2 mol mol−1). This work demonstrated that, in principle, SBE-β-CD could be used as efficient encapsulating agent for the (P)GKY20 or other antimicrobial peptides, rendering possible their pharmacological applications.

Keywords

Antimicrobial peptides Cyclodextrin Liposomes DSC Isothermal titration calorimetry 

Notes

Acknowledgements

We thank Dr. Marcella Niccoli for her technical support in the liposomes preparation procedure. We also thank the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany’s Excellence Strategy EXC-2033 Projektnummer 390677874 for financial support.

Supplementary material

10973_2019_8609_MOESM1_ESM.pdf (216 kb)
Supplementary material 1 (PDF 215 kb)

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Copyright information

© Akadémiai Kiadó, Budapest, Hungary 2019

Authors and Affiliations

  1. 1.Department of Chemical SciencesUniversity of Naples Federico II, Complesso Universitario di Monte Sant’AngeloNaplesItaly
  2. 2.Department of BiologyUniversity of Naples Federico IINaplesItaly
  3. 3.Physical Chemistry ITU Dortmund UniversityDortmundGermany

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