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Influence of the Shape of Nanostructured Metal Surfaces on Adsorption of Single Peptide Molecules in Aqueous Solution
Author(s) -
Feng Jie,
Slocik Joseph M.,
Sarikaya Mehmet,
Naik Rajesh R.,
Farmer Barry L.,
Heinz Hendrik
Publication year - 2012
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201102066
Subject(s) - adsorption , peptide , molecule , nanoparticle , aqueous solution , metal , random coil , crystallography , materials science , nanostructure , selective adsorption , chemistry , inorganic chemistry , chemical physics , nanotechnology , organic chemistry , circular dichroism , biochemistry
Self‐assembly and function of biologically modified metal nanostructures depend on surface‐selective adsorption; however, the influence of the shape of metal surfaces on peptide adsorption mechanisms has been poorly understood. The adsorption of single peptide molecules in aqueous solution (Tyr 12 , Ser 12 , A3, Flg‐Na 3 ) is investigated on even {111} surfaces, stepped surfaces, and a 2 nm cuboctahedral nanoparticle of gold using molecular dynamics simulation with the CHARMM‐METAL force field. Strong and selective adsorption is found on even surfaces and the inner edges of stepped surfaces (–20 to –60 kcal/mol peptide) in contrast to weaker and less selective adsorption on small nanoparticles (–15 to –25 kcal/mol peptide). Binding and selectivity appear to be controlled by the size of surface features and the extent of co‐ordination of epitaxial sites by polarizable atoms (N, O, C) along the peptide chain. The adsorption energy of a single peptide equals a fraction of the sum of the adsorption energies of individual amino acids that is characteristic of surface shape, epitaxial pattern, and conformation constraints (often β ‐strand and random coil). The proposed adsorption mechanism is supported and critically evaluated by earlier sequence data from phage display, dissociation constants of small proteins as a function of nanoparticle size, and observed shapes of peptide‐stabilized nanoparticles. Understanding the interaction of single peptides with shaped metal surfaces is a key step towards control over self‐organization of multiple peptides on shaped metal surfaces and the assembly of superstructures from nanostructures.