Control over Multiple Nano‐ and Secondary Structures in Peptide Self‐Assembly. (20th December 2021)
- Record Type:
- Journal Article
- Title:
- Control over Multiple Nano‐ and Secondary Structures in Peptide Self‐Assembly. (20th December 2021)
- Main Title:
- Control over Multiple Nano‐ and Secondary Structures in Peptide Self‐Assembly
- Authors:
- Ghosh, Goutam
Barman, Ranajit
Mukherjee, Anurag
Ghosh, Uttam
Ghosh, Suhrit
Fernández, Gustavo - Abstract:
- Abstract: Herein, we report the rich morphological and conformational versatility of a biologically active peptide (PEP‐1 ), which follows diverse self‐assembly pathways to form up to six distinct nanostructures and up to four different secondary structures through subtle modulation in pH, concentration and temperature. PEP‐1 forms twisted β‐sheet secondary structures and nanofibers at pH 7.4, which transform into fractal‐like structures with strong β‐sheet conformations at pH 13.0 or short disorganized elliptical aggregates at pH 5.5. Upon dilution at pH 7.4, the nanofibers with twisted β‐sheet secondary structural elements convert into nanoparticles with random coil conformations. Interestingly, these two self‐assembled states at pH 7.4 and room temperature are kinetically controlled and undergo a further transformation into thermodynamically stable states upon thermal annealing: whereas the twisted β‐sheet structures and corresponding nanofibers transform into 2D sheets with well‐defined β‐sheet domains, the nanoparticles with random coil structures convert into short nanorods with α‐helix conformations. Notably, PEP‐1 also showed high biocompatibility, low hemolytic activity and marked antibacterial activity, rendering our system a promising candidate for multiple bio‐applications. Abstract : We describe the nanostructural and conformational versatility of the biologically active peptide PEP‐1, which self‐assembles into up to six different aggregate morphologies andAbstract: Herein, we report the rich morphological and conformational versatility of a biologically active peptide (PEP‐1 ), which follows diverse self‐assembly pathways to form up to six distinct nanostructures and up to four different secondary structures through subtle modulation in pH, concentration and temperature. PEP‐1 forms twisted β‐sheet secondary structures and nanofibers at pH 7.4, which transform into fractal‐like structures with strong β‐sheet conformations at pH 13.0 or short disorganized elliptical aggregates at pH 5.5. Upon dilution at pH 7.4, the nanofibers with twisted β‐sheet secondary structural elements convert into nanoparticles with random coil conformations. Interestingly, these two self‐assembled states at pH 7.4 and room temperature are kinetically controlled and undergo a further transformation into thermodynamically stable states upon thermal annealing: whereas the twisted β‐sheet structures and corresponding nanofibers transform into 2D sheets with well‐defined β‐sheet domains, the nanoparticles with random coil structures convert into short nanorods with α‐helix conformations. Notably, PEP‐1 also showed high biocompatibility, low hemolytic activity and marked antibacterial activity, rendering our system a promising candidate for multiple bio‐applications. Abstract : We describe the nanostructural and conformational versatility of the biologically active peptide PEP‐1, which self‐assembles into up to six different aggregate morphologies and forms up to four different secondary structures in a controlled manner depending on pH, concentration, and temperature. … (more)
- Is Part Of:
- Angewandte Chemie. Volume 134:Number 5(2022)
- Journal:
- Angewandte Chemie
- Issue:
- Volume 134:Number 5(2022)
- Issue Display:
- Volume 134, Issue 5 (2022)
- Year:
- 2022
- Volume:
- 134
- Issue:
- 5
- Issue Sort Value:
- 2022-0134-0005-0000
- Page Start:
- n/a
- Page End:
- n/a
- Publication Date:
- 2021-12-20
- Subjects:
- amphiphilic systems -- self-assembly -- nanostructures -- peptides -- secondary structures
Chemistry -- Periodicals
540 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1002/ange.202113403 ↗
- Languages:
- English
- ISSNs:
- 0044-8249
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0902.000000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 25802.xml