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Research Article

The interaction between self – assembling peptides and emodin and the controlled release of emodin from in-situ hydrogel

, , , , , , , & show all
Pages 3961-3975 | Received 08 Mar 2019, Accepted 09 Sep 2019, Published online: 07 Oct 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.

Disclosure statement

No potential conflict of interest was reported by the authors.

Additional information

Funding

This work was supported by grants from the National Natural Science Foundation of China [No: 31460246], the Guizhou Provincial Science and Technology Foundation [No: Qiankehe LH [2014] 7564], the Project of Special Funds for Science and Technology Cooperation in Guizhou Provinces and Zunyi City (Shengshikehe [2015] 53), the Education Department of Guizhou Province [GNYL (2017) 006 and YLXKJS-YS-05], Collaborative Innovation Center of Guizhou Traditional Chinese Medicine and Ethnic medicine [No: Qianjiaokeyanfa [2012] 311], the National Key Research and Development Program of China [2016YFC1302203, JX Zhu] and the National Natural Science Foundation of China [81570695, 81370482, and 81270443].