Nanosized Complexes of the Proteolytic Enzyme Serratiopeptidase with Cationic Block Copolymer Micelles Enhance the Proliferation and Migration of Human Cells

Author:

Kamenova Katya1,Prancheva Anna1,Radeva Lyubomira2ORCID,Yoncheva Krassimira2ORCID,Zaharieva Maya M.3ORCID,Najdenski Hristo M.3ORCID,Petrov Petar D.1ORCID

Affiliation:

1. Institute of Polymers, Bulgarian Academy of Sciences, bl.103 Akad. G. Bonchev Str., 1113 Sofia, Bulgaria

2. Faculty of Pharmacy, Medical University of Sofia, 2 Dunav Str., 1000 Sofia, Bulgaria

3. The Stephan Angeloff Institute of Microbiology, 1113 Sofia, Bulgaria

Abstract

In this study, we describe the preparation of the cationic block copolymer nanocarriers of the proteolytic enzyme serratiopeptidase (SER). Firstly, an amphiphilic poly(2-(dimethylamino)ethyl methacrylate)-b-poly(ε-caprolactone)-b-poly(2-(dimethylamino)ethyl methacrylate) (PDMAEMA9-b-PCL35-b-PDMAEMA9) triblock copolymer was synthesized by reversible addition-fragmentation chain-transfer (RAFT) polymerization. Then, cationic micellar nanocarriers consisting of a PCL hydrophobic core and a PDMAEMA hydrophilic shell were formed by the solvent evaporation method. SER was loaded into the polymeric micelles by electrostatic interaction between the positively charged micellar shell and the negatively charged enzyme molecules. The particle size, zeta potential, and colloid stability of complexes as a function of SER concentration were investigated by dynamic and electrophoretic light scattering. It was found that SER retained its proteolytic activity after immobilization in polymeric carriers. Moreover, the complexes have a concentration-dependent enhancing effect on the proliferation and migration of human keratinocyte HaCaT and gingival fibroblast HGF cells.

Funder

Bulgarian National Science Fund

Publisher

MDPI AG

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