Serine Protease Inhibitors-New Molecules for Modification of Polymeric Biomaterials

Biomolecules. 2020 Jan 4;10(1):82. doi: 10.3390/biom10010082.

Abstract

Three serine protease inhibitors (AEBSF, soy inhibitor, α1-antitrypsin) were covalently immobilized on the surface of three polymer prostheses with the optimized method. The immobilization efficiency ranged from 11 to 51%, depending on the chosen inhibitor and biomaterial. The highest activity for all inhibitors was observed in the case of immobilization on the surface of the polyester Uni-Graft prosthesis, and the preparations obtained showed high stability in the environment with different pH and temperature values. Modification of the Uni-Graft prosthesis surface with the synthetic AEBSF inhibitor and human α1-antitrypsin inhibited the adhesion and multiplication of Staphylococcus aureus subs. aureus ATCC® 25923TM and Candida albicans from the collection of the Department of Genetics and Microbiology, UMCS. Optical profilometry analysis indicated that, after the immobilization process on the surface of AEBSF-modified Uni-Graft prostheses, there were more structures with a high number of protrusions, while the introduction of modifications with a protein inhibitor led to the smoothing of their surface.

Keywords: covalent immobilization; modification of biomaterials; protease inhibitors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Biocompatible Materials / chemical synthesis
  • Biocompatible Materials / pharmacology
  • Candida albicans / drug effects
  • Endopeptidases
  • Humans
  • Polymers
  • Serine Proteinase Inhibitors / chemistry*
  • Serine Proteinase Inhibitors / metabolism*
  • Serine Proteinase Inhibitors / pharmacology*
  • Staphylococcus aureus / drug effects
  • Sulfones / chemistry
  • Sulfones / pharmacology
  • alpha 1-Antitrypsin / chemistry
  • alpha 1-Antitrypsin / pharmacology

Substances

  • Anti-Bacterial Agents
  • Biocompatible Materials
  • Polymers
  • Serine Proteinase Inhibitors
  • Sulfones
  • alpha 1-Antitrypsin
  • 4-(2-aminoethyl)benzenesulfonylfluoride
  • Endopeptidases