Design of metal-binding sites onto self-assembled peptide fibrils

• Published in: Biopolymers Vol. 92; no. 3; pp. 164 - 172
• Main Authors: Kasotakis, Emmanouil, Mossou, Estelle, Adler-Abramovich, Lihi, Mitchell, Edward P., Forsyth, V. Trevor, Gazit, Ehud, Mitraki, Anna
• Format: Journal Article
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 2009
• Subjects: Adenovirus; Amyloid beta-Peptides - chemistry; Binding Sites; biological materials; Drug Design; Gold - chemistry; Nanoparticles - chemistry; nanowires; peptides; Peptides - chemistry; Platinum - chemistry; protein design; self-assembly; Silver - chemistry
• ISSN: 0006-3525; 1097-0282
• DOI: 10.1002/bip.21163

The ability to develop a rational basis for the binding of inorganic materials to specific binding sites within self‐assembling biological scaffolds has important applications in nanobiotechnology. Amyloid‐forming peptides are a class of such scaffolds and show enormous potential as templates for the fabrication of low resistance, conducting nanowires. Here we report the use of a self‐assembling peptide building block as scaffold for the systematic introduction of metal‐binding residues at specific locations within the structure. The octapeptide NSGAITIG (Asparagine‐Serine‐Glycine‐Alanine‐Isoleucine‐Threonine‐Isoleucine‐Glycine) from the fiber protein of adenovirus has been identified in previous structural studies as an elementary fibril‐forming building block. Using this building block as a scaffold, we have designed three new cysteine‐containing octa‐peptides to study their eventual fibril‐forming ability and potential templating of metal nanoparticles. We find that the cysteine substitutions do not alter the fibril‐forming potential of the peptides, and that the fibrils formed bind efficiently to silver, gold, and platinum nanoparticles; furthermore, we report unexpected behavior of serine in nucleating gold and platinum nanoparticles. We find that combination of cysteine and serine residues projecting from adjacent sites on a peptide scaffold represents a potentially useful strategy in nucleating inorganic materials. The ability to reliably produce metal‐coated fibrils is a vital first step towards the exploitation of these fibrils as conducting nanowires with applications in nano‐circuitry. Short, biologically inspired self‐assembling peptide scaffolds derived from natural fibrous proteins with known three‐dimensional structure may provide a viable approach towards the rational design of inorganic nanowires. © 2009 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 92: 164–172, 2009.
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