Insights on the Facet Specific Adsorption of Amino Acids and Peptides toward Platinum

Abstract

Engineering shape-controlled bionanomaterials requires comprehensive understanding of interactions between biomolecules and inorganic surfaces. We explore the origin of facet-selective binding of peptides adsorbed onto Pt(100) and Pt(111) crystallographic planes. Using molecular dynamics simulations, we show that upon adsorption the peptides adopt a predictable conformation. We compute the binding energies of the amino acids constituting two adhesion peptides for Pt, S7, and T7 and demonstrate that peptides' surface recognition behavior that makes them unique among populations originates from differential adsorption of their building blocks. We find that the degree of peptide binding is mainly due to polar amino acids and the molecular architecture of the peptides close to the Pt facets. Our analysis is a first step in the prediction of enhanced affinity between inorganic materials and a peptides, toward the synthesis of novel nanomaterials with programmable shape, structure, and properties.

Organic–inorganic interface simulation for new material discoveries

“…Our group employed the DFT and MD simulations to investigate the mechanism of both the amino acids and peptide against the platinum(1 0 0) and Pt(1 1 1) crystallographic facets. We found that phenyl alanine (F) is the main contributor for the Pt(1 1 1) facet specificity whereas Leu and Thr contribute for Pt(1 0 0) . Ruan et al integrated the Pt(1 1 1) facet‐specific amino acid, Phe(F), into a nonspecific peptide and turned the nonspecific peptide to a specific one and produced nanocrystals of desired shape (Figure ) .…”

“…In the case of protein–surface interactions, most of the DFT simulation studies are limited to a single amino acid or small di‐ and tri‐peptide with a few hundred surface atoms . However, it can provide meaningful data for parameterizing MM force fields (FFs).…”

“…A large number of computational studies were performed on the interface between protein and metal surfaces, such as Au( 1 0 0), Au(1 1 1), Pd, Pt,, and Ni . Heinz et al studied the selective binding of several short peptides to surfaces of Au, Pd, and Pd–Au bimetal using a CVFF FF with derived LJ parameters.…”

“…A hexagonal spacing of ∼1.6 Å between available lattice sites on the (1 1 1) surfaces show the preference for aromatic rings and a quadratic spacing of ∼2.8 Å favor only small molecule such as water or engineered repeats as shown in Figure . Our group has studied the affinity of amino acids that constitute the facet‐specific peptides derived from phage display technique, S7 (Ac‐Ser‐Ser‐Phe‐Pro‐Gln‐Pro‐Asn‐CONH 2 ) and T7 (Ac‐Thr‐Leu‐Thr‐Thr‐Leu‐Thr‐Asn‐CONH 2 ) against the Pt(1 1 1) and Pt(1 0 0) crystallographic facets by MD simulations using classical CVFF and CVFF with modified LJ parameters from Refs and . We found that the trend of adsorption behavior between both CVFF models does not change, but the adsorption energies in the modified CVFF are far better and more realistic.…”

Nanocrystal facet modulation to enhance transferrin binding and cellular delivery

“…For example, thermal hysteresis proteins, a group of serum proteins commonly present in organisms living in cold environments, bind to specific faces of ice crystals to enable their antifreeze activity 13,14 . Recent theoretical studies point to the possibility of facet-dependent selective binding of amino acids, peptides, proteins, and DNA to crystal surfaces containing metals [15][16][17][18][19] . Here, we experimentally prove the concept that facet engineering may be utilized to tune the nanocrystal-biomolecule association for refining biological applications of crystalline nanomaterials.…”