Metal‐Coordinated Supramolecular Polymers from the Minimalistic Hybrid Peptide Foldamers. (18th March 2021)
- Record Type:
- Journal Article
- Title:
- Metal‐Coordinated Supramolecular Polymers from the Minimalistic Hybrid Peptide Foldamers. (18th March 2021)
- Main Title:
- Metal‐Coordinated Supramolecular Polymers from the Minimalistic Hybrid Peptide Foldamers
- Authors:
- Dey, Sanjit
Misra, Rajkumar
Saseendran, Abhijith
Pahan, Saikat
Gopi, Hosahudya N. - Abstract:
- Abstract: Availing the peptide folded architectures to design metal‐coordinated frameworks and cages is restricted due to the scarcity of readily accessible short and stable secondary structures. The secondary structures, α‐helix and β‐sheets, play significant roles in stabilizing tertiary folds of proteins. Designing such helical structures from the short sequences of peptides without having any steric restrictions is exceptionally challenging. Here we reveal the short α, γ‐hybrid tripeptide sequences that manifest stable helical structures without having any sterically constrained amino acids. These short hybrid tripeptides fold into helices even in the presence of two typically β‐sheet favoring Val residues. The hybrid helix consisting of terminal pyridine units coordinates with the metal ions and drives the helical polymerization. Depending on the sequence and the position of N in pyridine moieties, these peptides form selective metallogels with Ag + and Cu 2+ ions. The X‐ray diffracted analysis of the peptide single crystals obtained from the gel matrix reveals that the helical structure is maintained during the self‐assembly process. Further, by varying the counter anion, a 3D helical crystalline coordination polymer with permanent porosity is generated. The findings reported here can be used to design new functional metal‐foldamer coordinated polymers. Abstract : Metal‐mediated supramolecular assembly of short helical peptides is investigated. Sequence specificAbstract: Availing the peptide folded architectures to design metal‐coordinated frameworks and cages is restricted due to the scarcity of readily accessible short and stable secondary structures. The secondary structures, α‐helix and β‐sheets, play significant roles in stabilizing tertiary folds of proteins. Designing such helical structures from the short sequences of peptides without having any steric restrictions is exceptionally challenging. Here we reveal the short α, γ‐hybrid tripeptide sequences that manifest stable helical structures without having any sterically constrained amino acids. These short hybrid tripeptides fold into helices even in the presence of two typically β‐sheet favoring Val residues. The hybrid helix consisting of terminal pyridine units coordinates with the metal ions and drives the helical polymerization. Depending on the sequence and the position of N in pyridine moieties, these peptides form selective metallogels with Ag + and Cu 2+ ions. The X‐ray diffracted analysis of the peptide single crystals obtained from the gel matrix reveals that the helical structure is maintained during the self‐assembly process. Further, by varying the counter anion, a 3D helical crystalline coordination polymer with permanent porosity is generated. The findings reported here can be used to design new functional metal‐foldamer coordinated polymers. Abstract : Metal‐mediated supramolecular assembly of short helical peptides is investigated. Sequence specific selective metallogels with different metal ions, two‐dimensional metal‐coordinated helical polymers, and three‐dimensional metal‐helix porous frameworks are reported. Studies suggested that short hybrid helical peptides can be used to construct metal‐mediated architectures. … (more)
- Is Part Of:
- Angewandte Chemie. Volume 133:Number 18(2021)
- Journal:
- Angewandte Chemie
- Issue:
- Volume 133:Number 18(2021)
- Issue Display:
- Volume 133, Issue 18 (2021)
- Year:
- 2021
- Volume:
- 133
- Issue:
- 18
- Issue Sort Value:
- 2021-0133-0018-0000
- Page Start:
- 9951
- Page End:
- 9956
- Publication Date:
- 2021-03-18
- Subjects:
- foldamers -- metal-folded 3D porous polymer -- metal-peptide folding -- supramolecular polymerization -- X-ray diffraction
Chemistry -- Periodicals
540 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1002/ange.202015838 ↗
- 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:
- 16729.xml