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The interaction between self – assembling peptides and emodin and the controlled release of emodin from in-situ hydrogel.
- Source :
-
Artificial Cells, Nanomedicine & Biotechnology . Dec2019, Vol. 47 Issue 1, p3961-3975. 15p. - Publication Year :
- 2019
-
Abstract
- Ion-complementary self-assembling peptides have potential in delivering hydrophobic drugs. This study involved two self-assembling peptides, RADA16-I and RVDV16-I, of which RVDV16-I was a novel self-assembling peptide with different hydrophobic side chains designed from RADA16-I. The purpose of this study was to observe the interaction between different self-assembling peptides and emodin through fluorescence spectrophotometry, CD, SEM and AFM; to construct a preliminary suspension in-situ hydrogel delivery system for emodin with the self-assembling peptides; and to investigate the drug-loading and drug-releasing properties of the self-assembling peptides on emodin. The results showed that both peptides can interact with emodin and the interaction was dominated by hydrophobic interaction. The aqueous solutions of both self-assembling peptides can form relatively stable suspensions with emodin under mechanical stirring, and the suspension can form in-situ hydrogel under physiological condition. In vitro release of emodin from the hydrogels showed a manner of sustained release to some extent. Cell viability studies showed inherent proliferation inhibiting effects of emodin on tumor cells was maintained or enhanced through the in-situ hydrogels. The self-assembling peptides RADA16-I and RVDV16-I had showed promising drug-loading and drug-releasing performance for hydrophobic drugs. It is reasonable to exploit self-assembling peptides as drug carriers for their great potential to improve delivery of hydrophobic drugs. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 21691401
- Volume :
- 47
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Artificial Cells, Nanomedicine & Biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 145014702
- Full Text :
- https://doi.org/10.1080/21691401.2019.1673768