Enhancement of electronic effects at a biomolecule–inorganic interface by multivalent interactions. Issue 4 (10th January 2023)
- Record Type:
- Journal Article
- Title:
- Enhancement of electronic effects at a biomolecule–inorganic interface by multivalent interactions. Issue 4 (10th January 2023)
- Main Title:
- Enhancement of electronic effects at a biomolecule–inorganic interface by multivalent interactions
- Authors:
- Kramer, Naomi
Sivron, Ido
Le Saux, Guillaume
Mendieta-Moreno, Jesús I.
Ashkenasy, Nurit - Abstract:
- Abstract : The multivalency of basic peptides influences the level of binding to indium tin oxide (ITO) and the extent of reduction of the work function, paving the way for amelioration of the performance of optoelectronic devices by using sustainable coatings. Abstract : The binding of peptides and proteins through multiple weak interactions is ubiquitous in nature. Biopanning has been used to "hijack" this multivalent binding for the functionalization of surfaces. For practical applications it is important to understand how multivalency influences the binding interactions and the resulting behaviour of the surface. Considering the importance of optimization of the electronic properties of surfaces in diverse electronic and optoelectronic applications, we study here the relation between the multivalency effect and the resulting modulation of the surface work function. We use 12-mer peptides, which were found to strongly bind to oxide surfaces, to functionalize indium tin oxide (ITO) surfaces. We show that the affinity of the peptides for the ITO surface, and concurrently the effect on the ITO work function, are linearly affected by the number of basic residues in the sequence. The multivalent binding interactions lead to a peptide crowding effect, and a stronger modulation of the work function for adodecapeptide than for a single basic amino acid functionalization. The bioderived molecular platform presented herein can pave the way to a novel approach to improve theAbstract : The multivalency of basic peptides influences the level of binding to indium tin oxide (ITO) and the extent of reduction of the work function, paving the way for amelioration of the performance of optoelectronic devices by using sustainable coatings. Abstract : The binding of peptides and proteins through multiple weak interactions is ubiquitous in nature. Biopanning has been used to "hijack" this multivalent binding for the functionalization of surfaces. For practical applications it is important to understand how multivalency influences the binding interactions and the resulting behaviour of the surface. Considering the importance of optimization of the electronic properties of surfaces in diverse electronic and optoelectronic applications, we study here the relation between the multivalency effect and the resulting modulation of the surface work function. We use 12-mer peptides, which were found to strongly bind to oxide surfaces, to functionalize indium tin oxide (ITO) surfaces. We show that the affinity of the peptides for the ITO surface, and concurrently the effect on the ITO work function, are linearly affected by the number of basic residues in the sequence. The multivalent binding interactions lead to a peptide crowding effect, and a stronger modulation of the work function for adodecapeptide than for a single basic amino acid functionalization. The bioderived molecular platform presented herein can pave the way to a novel approach to improve the performance of optoelectronic devices in an eco-friendly manner. … (more)
- Is Part Of:
- Physical chemistry chemical physics. Volume 25:Issue 4(2023)
- Journal:
- Physical chemistry chemical physics
- Issue:
- Volume 25:Issue 4(2023)
- Issue Display:
- Volume 25, Issue 4 (2023)
- Year:
- 2023
- Volume:
- 25
- Issue:
- 4
- Issue Sort Value:
- 2023-0025-0004-0000
- Page Start:
- 3251
- Page End:
- 3257
- Publication Date:
- 2023-01-10
- Subjects:
- Chemistry, Physical and theoretical -- Periodicals
541.3 - Journal URLs:
- http://pubs.rsc.org/en/journals/journalissues/cp#!issueid=cp016040&type=current&issnprint=1463-9076 ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d2cp03679g ↗
- Languages:
- English
- ISSNs:
- 1463-9076
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6475.306000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 25719.xml