Higher-order complexity through R-group effects in self-assembled tripeptide monolayers.
Self-assembled monolayers of tri-L-leucine and tri-L-valine formed on highly ordered pyrolytic graphite (HOPG) substrates have been examined using scanning tunneling microscopy. These monolayers exhibit markedly different structures, even though the tripeptides differ by only a minor change in the amino acid R-group. This minor change in R-group apparently affects the balance between hydrogen bonding and van der Waals interactions that control the monolayer structures. Implications of this effect for evolution of molecular complexity in prebiotic synthesis on environmental surfaces are discussed.
Rampulla
David M
DM
Department of Chemistry, Princeton University, Princeton, New Jersey 08544, USA.
Oncel
Nuri
N
Malcolm
Stuart A
SA
Bernasek
Steven L
SL
D000327:Adsorption; D002244:Carbon / Q000737:chemistry*; D007930:Leucine / Q000138:chemical synthesis* / Q000737:chemistry; D008567:Membranes, Artificial; D016252:Microscopy, Scanning Tunneling; D008958:Models, Molecular; D008968:Molecular Conformation; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry; D010316:Particle Size; D013499:Surface Properties; D014633:Valine / Q000138:chemical synthesis* / Q000737:chemistry
D008567:Membranes, Artificial; D009842:Oligopeptides; C009139:pyrolytic carbon; D002244:Carbon; D007930:Leucine; D014633:Valine