Glycoconjugate nanoribbons from the self-assembly of carbohydrate-peptide block molecules for controllable bacterial cell cluster formation.
We demonstrate here the rational design strategy to control the length of 1-dimensional beta-sheet peptide nanoassembly. We synthesized the beta-sheet peptides with attached coils and carbohydrates. We reasoned that the bulkiness of the coils affects the final length of the assembled beta-sheet peptide nanostructures because of the steric crowding effect. The nanostructure from the peptide with a small and linear coil was several micrometers long, whereas the one from the peptide with a high-volume-fraction dendritic coil was only about 150 nm long. For potential biological applications of the peptide nanoassemblies, we investigated the interactions of the carbohydrate-coated nanoassemblies with E. coli cells containing cognate binding proteins. The results showed that both of the nanoassemblies could immobilize and/or aggregate bacterial cells. The degrees of immobilization were similar for both nanoassemblies; however, only the long nanoribbon was shown to induce the formation of bacterial clusters.
Lim
Yong-Beom
YB
Center for Supramolecular Nano-Assembly and Department of Chemistry, and Department of Biochemistry, Yonsei University, Seoul 120-749, Korea.
Park
Somi
S
Lee
Eunji
E
Jeong
Haemi
H
Ryu
Ja-Hyoung
JH
Lee
Myeong Sup
MS
Lee
Myongsoo
M
D001419:Bacteria / Q000737:chemistry*; D002241:Carbohydrates / Q000737:chemistry; D018914:Cells, Immobilized / Q000737:chemistry; D004926:Escherichia coli / Q000737:chemistry; D006020:Glycopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D049329:Nanostructures / Q000737:chemistry*; D017433:Protein Structure, Secondary
D002241:Carbohydrates; D006020:Glycopeptides