Pomegranate seed polyphenol-based nanosheets as an efficient inhibitor of amyloid fibril assembly and cytotoxicity of HEWL. Issue 14 (21st March 2022)
- Record Type:
- Journal Article
- Title:
- Pomegranate seed polyphenol-based nanosheets as an efficient inhibitor of amyloid fibril assembly and cytotoxicity of HEWL. Issue 14 (21st March 2022)
- Main Title:
- Pomegranate seed polyphenol-based nanosheets as an efficient inhibitor of amyloid fibril assembly and cytotoxicity of HEWL
- Authors:
- Meratan, Ali Akbar
Hassani, Vahid
Mahdavi, Atiyeh
Nikfarjam, Nasser - Abstract:
- Abstract : PFPS nanosheets modulate the amyloid fibrillation of HEWL much more effective than the bulk form of PFPS. Based on the thioflavin T results, a delay in the initiation of the assembly process appears to be the mechanism of action of PFPS nanosheets. Abstract : Poor water solubility and low bioavailability are considered as two main factors restricting therapeutic applications of natural polyphenols in relation to various disorders including amyloid-related diseases. Among various strategies developed to overcome these limitations, nanonization has attracted considerable attention. Herein, we compared the potency of bulk and nano forms of the polyphenolic fraction of pomegranate seed (PFPS) for modulating Hen Egg White Lysozyme (HEWL) amyloid fibril formation. Prepared PFPS nanosheets using direct oxidative pyrolysis were characterized by employing a range of spectroscopic and microscopic techniques. We found that the nano form can inhibit the assembly process and disintegrate preformed fibrils of HEWL much more effective than the bulk form of PFPS. Moreover, MTT-based cell viability and hemolysis assays showed the capacity of both bulk and nano forms of PFPS in attenuating HEWL amyloid fibril-induced toxicity, where the nano form was more effective. On the basis of thioflavin T results, a delay in the initiation of amyloid fibril assembly of HEWL appears to be the mechanism of action of PFPS nanosheets. We suggest that the improved efficiency of PFPS nanosheets inAbstract : PFPS nanosheets modulate the amyloid fibrillation of HEWL much more effective than the bulk form of PFPS. Based on the thioflavin T results, a delay in the initiation of the assembly process appears to be the mechanism of action of PFPS nanosheets. Abstract : Poor water solubility and low bioavailability are considered as two main factors restricting therapeutic applications of natural polyphenols in relation to various disorders including amyloid-related diseases. Among various strategies developed to overcome these limitations, nanonization has attracted considerable attention. Herein, we compared the potency of bulk and nano forms of the polyphenolic fraction of pomegranate seed (PFPS) for modulating Hen Egg White Lysozyme (HEWL) amyloid fibril formation. Prepared PFPS nanosheets using direct oxidative pyrolysis were characterized by employing a range of spectroscopic and microscopic techniques. We found that the nano form can inhibit the assembly process and disintegrate preformed fibrils of HEWL much more effective than the bulk form of PFPS. Moreover, MTT-based cell viability and hemolysis assays showed the capacity of both bulk and nano forms of PFPS in attenuating HEWL amyloid fibril-induced toxicity, where the nano form was more effective. On the basis of thioflavin T results, a delay in the initiation of amyloid fibril assembly of HEWL appears to be the mechanism of action of PFPS nanosheets. We suggest that the improved efficiency of PFPS nanosheets in modulating the HEWL fibrillation process may be attributed to their increased surface area in accord with the surface-assistance model. Our results may present polyphenol-based nanosheets as a powerful approach for drug design against amyloid-related diseases. … (more)
- Is Part Of:
- RSC advances. Volume 12:Issue 14(2022)
- Journal:
- RSC advances
- Issue:
- Volume 12:Issue 14(2022)
- Issue Display:
- Volume 12, Issue 14 (2022)
- Year:
- 2022
- Volume:
- 12
- Issue:
- 14
- Issue Sort Value:
- 2022-0012-0014-0000
- Page Start:
- 8719
- Page End:
- 8730
- Publication Date:
- 2022-03-21
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d1ra05820g ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 21485.xml