| Autor: |
Kalita, Mrinal, Yadav, Khushboo, Archana, Archana, Gopakumar, Thiruvancheril G., Vasudev, Prema G., Ramapanicker, Ramesh |
| Zdroj: |
Journal of Peptide Science; Nov2024, Vol. 30 Issue 11, p1-8, 8p |
| Abstrakt: |
The possibility of introducing various functionalities on peptides with relative ease allows them to be used for molecular applications. However, oligopeptides prepared entirely from proteinogenic amino acids seldom assemble as ordered structures on surfaces. Therefore, sidechain modifications of peptides that can increase the intermolecular interactions without altering the constitution of a given peptide become an attractive route to self‐assembling them on surfaces. We find that replacing phenylalanine residues with unusual amino acids that have phenylcarbonyl sidechains in oligopeptides increases the formation of ordered self‐assembly on a highly ordered pyrolytic graphite surface. Peptides containing the modified amino acids provided extended long‐range ordered assemblies, while the analogous peptides containing phenylalanine residues failed to form long‐range assemblies. X‐ray crystallographic analysis of the bulk structures of these peptides and the analogous peptides containing phenylalanine residues reveal that such modifications do not alter the secondary structure in crystals. It also reveals that the secondary hydrogen bonding interaction through phenylcarbonyl sidechains facilitates extended growth of the peptides on graphite. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
Plný text