Hydrolytic nondegradable bioactive rosmarinic acid particles

Şahiner M.

POLYMERS FOR ADVANCED TECHNOLOGIES, vol.32, no.12, pp.4891-4901, 2021 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 32 Issue: 12
  • Publication Date: 2021
  • Doi Number: 10.1002/pat.5481
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, PASCAL, Aerospace Database, Applied Science & Technology Source, Chemical Abstracts Core, Chimica, Communication Abstracts, Compendex, INSPEC, Metadex, Civil Engineering Abstracts
  • Page Numbers: pp.4891-4901
  • Keywords: antimicrobial, antioxidant, nano, micro particles, nondegradable particles, phenolic acid, rosmarinic acid, SODIUM TRIMETAPHOSPHATE, ANTIOXIDANT
  • Çanakkale Onsekiz Mart University Affiliated: Yes


Rosmarinic acid (RS) is as the nonflavonoid polyphenols in the phenolic acid subgroup was cross-linked with sodium trimetaphosphate (STMP) to obtain (p[RS-co-STMP]) particles with the size distribution of 2.992 +/- 659 nm. The zeta potential values of p(RS-co-STMP) particles were measured between pH 2-10, and the isoelectric point was determined as pH 2.66. Fe(II) chelating capability test was done for RS and p(RS-co-STMP). At 800 mu mol/ml concentrations, p(RS-co-STMP) particles chelated 95.06 +/- 5.18% Fe(II), while RS molecule did not chelate Fe(II), whereas STMP chelated only 41.8 +/- 5.9% Fe(II). The effects of RS and p(RS-co-STMP) particles on alpha-glucosidase enzyme activity were investigated and were found to inhibit the alpha-glucosidase enzyme by 55.7% and 89.6%, respectively. Furthermore, p(RS-co-STMP) particles were modified with polyethyleneimine as m-p(RS-co-STMP) to improve antimicrobial properties and found effective against both Escherichia coli and Staphylococcus aureus bacteria. The interaction of fibrinogen with RS, p(RS-co-STMP) and m-p(RS-co-STMP) were studied via the change in intensity of corresponding fluorescence spectra. It was found that p(RS-co-STMP) particles interacted lesser with fibrinogen than RS and changed the fluorescence property of fibrinogen protein slightly. On the other hand, m-p(RS-co-STMP) particles did not change the fluorescence intensity of fibrinogen suggesting no influence on the blood clotting.