Sequence-directed organization of beta-peptides in self-assembled monolayers.
The sequence-directed organization of self-assembled monolayers of amphiphilic beta-peptides adsorbed on gold surfaces is studied using Monte Carlo simulations. A phenomenological model is presented in which each (helical) molecule is represented by a rigid nanorod; side groups are placed at appropriate locations. This model can distinguish between globally amphiphilic (GA) and nonglobally amphiphilic (iso-GA) sequence isomers. The simulations show that the GA isomers have a high degree of orientational order that is not exhibited by the iso-GA isomers, which is consistent with experiment (Pomerantz et al. Chem. Mater. 2007, 19, 4436). The effect of surface coverage and relative strength of electrostatic, hydrophilic, and hydrophobic interactions on the self-assembly of beta-peptides is quantified.
Mondal
Jagannath
J
Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
Sung
Bong June
BJ
Yethiraj
Arun
A
D000327:Adsorption; D000595:Amino Acid Sequence; D003198:Computer Simulation; D006046:Gold / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D007536:Isomerism; D008958:Models, Molecular; D009010:Monte Carlo Method; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D055672:Static Electricity; D013499:Surface Properties
D010455:Peptides; D006046:Gold