Comparative study of materials-binding peptide interactions with gold and silver surfaces and nanostructures : A thermodynamic basis for biological selectivity of inorganic materials

Palafox-Hernandez,JP, Tang,Z, Hughes,ZE, Li,Y, Swihart,MT, Prasad,PN, Walsh,TR and Knecht,MR 2014, Comparative study of materials-binding peptide interactions with gold and silver surfaces and nanostructures : A thermodynamic basis for biological selectivity of inorganic materials, Chemistry of Materials, vol. 26, no. 17, pp. 4960-4969, doi: 10.1021/cm501529u.

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Title Comparative study of materials-binding peptide interactions with gold and silver surfaces and nanostructures : A thermodynamic basis for biological selectivity of inorganic materials
Author(s) Palafox-Hernandez,JP
Tang,Z
Hughes,ZEORCID iD for Hughes,ZE orcid.org/0000-0003-2166-9822
Li,Y
Swihart,MT
Prasad,PN
Walsh,TRORCID iD for Walsh,TR orcid.org/0000-0002-0233-9484
Knecht,MR
Journal name Chemistry of Materials
Volume number 26
Issue number 17
Start page 4960
End page 4969
Total pages 10
Publisher American Chemical Society
Place of publication Washington, United States
Publication date 2014-09-09
ISSN 0897-4756
1520-5002
Keyword(s) Science & Technology
Physical Sciences
Technology
Chemistry, Physical
Materials Science, Multidisciplinary
Chemistry
Materials Science
NANOPARTICLE SUPERLATTICES
ADSORPTION
SIMULATION
DISPLAY
PROTEIN
IDENTIFICATION
SPECTROSCOPY
ASSEMBLIES
NANOWIRES
EFFICIENT
Summary Controllable 3D assembly of multicomponent inorganic nanomaterials by precisely positioning two or more types of nanoparticles to modulate their interactions and achieve multifunctionality remains a major challenge. The diverse chemical and structural features of biomolecules can generate the compositionally specific organic/inorganic interactions needed to create such assemblies. Toward this aim, we studied the materials-specific binding of peptides selected based upon affinity for Ag (AgBP1 and AgBP2) and Au (AuBP1 and AuBP2) surfaces, combining experimental binding measurements, advanced molecular simulation, and nanomaterial synthesis. This reveals, for the first time, different modes of binding on the chemically similar Au and Ag surfaces. Molecular simulations showed flatter configurations on Au and a greater variety of 3D adsorbed conformations on Ag, reflecting primarily enthalpically driven binding on Au and entropically driven binding on Ag. This may arise from differences in the interfacial solvent structure. On Au, direct interaction of peptide residues with the metal surface is dominant, while on Ag, solvent-mediated interactions are more important. Experimentally, AgBP1 is found to be selective for Ag over Au, while the other sequences have strong and comparable affinities for both surfaces, despite differences in binding modes. Finally, we show for the first time the impact of these differences on peptide mediated synthesis of nanoparticles, leading to significant variation in particle morphology, size, and aggregation state. Because the degree of contact with the metal surface affects the peptide's ability to cap the nanoparticles and thereby control growth and aggregation, the peptides with the least direct contact (AgBP1 and AgBP2 on Ag) produced relatively polydispersed and aggregated nanoparticles. Overall, we show that thermodynamically different binding modes at metallic interfaces can enable selective binding on very similar inorganic surfaces and can provide control over nanoparticle nucleation and growth. This supports the promise of bionanocombinatoric approaches that rely upon materials recognition.
Language eng
DOI 10.1021/cm501529u
Field of Research 030603 Colloid and Surface Chemistry
030704 Statistical Mechanics in Chemistry
100703 Nanobiotechnology
Socio Economic Objective 970110 Expanding Knowledge in Technology
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2014, American Chemical Society
Persistent URL http://hdl.handle.net/10536/DRO/DU:30069080

Document type: Journal Article
Collections: Institute for Frontier Materials
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