Uncovering the design rules for peptide synthesis of metal nanoparticles

Journal of the American Chemical Society

Volumn 132, Issue 16, 2010, Pages 5677-5686

  Tan, Yen Nee ^a   Lee, Jim Yang ^a   Wang, Daniel I C ^a,b  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^b Massachusetts Institute of Technology Cambridge   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; AMINO ACID SEQUENCE; AU NANOPARTICLE; BINDING STRENGTH; BIOCOMPATIBLE METALS; BIOLOGICAL SOURCES; CAPPING AGENT; DESIGN RULES; GOLD NANOPARTICLES; KNOWLEDGE EXTRACTION; METAL NANOPARTICLES; METAL NANOSTRUCTURE; MULTIFUNCTIONAL REAGENTS; NANOPLATES; NET CHARGES; NUCLEATION AND GROWTH; PEPTIDE DESIGN; PEPTIDE SEQUENCES; PEPTIDE SYNTHESIS; RATIONAL DESIGN; SHAPE-CONTROLLED; STRATEGIC PLACEMENT;

AMINO ACIDS; DESIGN; GOLD; METAL RECOVERY; METALS; NANOPARTICLES; ORGANIC ACIDS; SYNTHESIS (CHEMICAL);

PEPTIDES;

ALPHA AMINO ACID; AMINO ACID; GOLD CHLORIDE; GOLD NANOPARTICLE; METAL NANOPARTICLE; NANOSPHERE; PEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BIOCOMPATIBILITY; BIOMINERALIZATION; CONTROLLED STUDY; METAL BINDING; METHODOLOGY; NONHUMAN; PEPTIDE SYNTHESIS; PROTEIN BINDING; PROTEIN STRUCTURE; CHEMISTRY; DRUG DESIGN; KINETICS; OXIDATION REDUCTION REACTION; PARTICLE SIZE; STRUCTURE ACTIVITY RELATION; SYNTHESIS;

AMINO ACID SEQUENCE; DRUG DESIGN; KINETICS; METAL NANOPARTICLES; OXIDATION-REDUCTION; PARTICLE SIZE; PEPTIDES; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 77952565030     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja907454f     Document Type: Article

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46. A is the binding constant.
47. For ease of visualization, the binding rating, which is the equilibrium surface coverage of the peptide in question on gold normalized by the equilibrium surface coverage of QHQHQHQ, was multiplied by a factor of 3 (Figure 3 c).
48. Based on the rating scheme I in Figure 2 using XWXWXWX peptide.
49. Since W was used as the common reducing residue in the W-X peptide sequence, the major difference between the reduction capabilities of the 20 interdigitated peptides should be contributed by the X residue. However, it was found that the reduction capability of a W-X peptide is not a linear sum of the capabilities of its amino acid constituents. For example, tyrosine (Y), which showed fairly good reduction capability on its own, actually downgraded the reactivity of W more so than other amino acids when it was incorporated as the W-Y sequence (Figure 2 b). This result shows that the intrinsic reduction property of an amino acid (X) is less influential than its binding affinity in affecting the overall reduction performance of an interdigitated peptide. This is even true when the strongest reducing amino acid (i.e., W) was used as the common interdigitated residue. Hence, the Δ H contribution from the intrinsic reduction capability of X is minor compared to the Δ S contribution, and the Δ G in the peptide reduction of metal precursor is controlled by the entropy effect.
50. 7. This is because the smaller number of gold-binding sites (two vs seven) would not impose a strong compensational effect on gold ion reduction.
51. We have also carried out experiments in which a single amino acid residue (W, Y, or F) was inserted between the shape-directing sequences. The self-regulation effect was absent in this case, and the reduction rate follows the reduction capability of the inserted residue, decreasing in the following order: SEKL W GASL > SEKL Y GASL > SEKL F GASL. Hence, self-regulation in a homodipeptide sequence would elevate the more prominent feature of the amino acid involved (e.g., for W, it is the reduction capability).