STM vizualization of thiol-containing peptide dendrimers on Au(111).
Peptide dendrimers assembled by solid-phase peptide synthesis using a branching diamino acid at every 2(nd) or 3(rd) position provide readily accessible synthetic model systems for proteins and enzymes. They adopt a globular shape by topology rather than by folding. Peptide dendrimers of 2(nd) and 3(rd) generation functionalized with a cysteine or cystine residue in the core were adsorbed on Au(111) surface and imaged by STM at air, under UHV, or in solution. The dendrimers appear as globular features with dimensions suggesting an extended flattened conformation, forming both single globules and ordered arrays on the surface. These images represent the first direct visualization of peptide dendrimer enzyme models.
Delort
Estelle
E
Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, CH-3012 Bern, Switzerland.
Szöcs
Edit
E
Widmer
Roland
R
Siegenthaler
Hans
H
Reymond
Jean-Louis
JL
D000388:Air; D001274:Atmospheric Pressure; D050091:Dendrimers / Q000737:chemistry*; D004572:Electrolysis; D006046:Gold / Q000737:chemistry*; D016252:Microscopy, Scanning Tunneling; D010455:Peptides / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000737:chemistry*
D050091:Dendrimers; D010455:Peptides; D013438:Sulfhydryl Compounds; D006046:Gold