Peptide-functionalized semiconductor surfaces: strong surface electronic effects from minor alterations to backbone composition.

The use of non-canonical amino acids is a powerful way to control protein structure. Here, we show that subtle changes to backbone composition affect the ability of a dipeptide to modify solid surface electronic properties. The extreme sensitivity of the interactions to the peptide structure suggests potential applications in improving the performance of electronic devices.

Filling the Green Gap of a Megadalton Photosystem I Complex by Conjugation of Organic Dyes.

Photosynthesis is Nature's major process for converting solar into chemical energy. One of the key players in this process is the multiprotein complex photosystem I (PSI) that through absorption of incident photons enables electron transfer, which makes this protein attractive for applications in bioinspired photoactive hybrid materials. However, the efficiency of PSI is still limited by its poor absorption in the green part of the solar spectrum. Inspired by the existence of natural phycobilisome light-harvesting antennae, we have widened the absorption spectrum of PSI by covalent attachment of synthetic dyes to the protein backbone. Steady-state and time-resolved photoluminescence reveal that energy transfer occurs from these dyes to PSI. It is shown by oxygen-consumption measurements that subsequent charge generation is substantially enhanced under broad and narrow band excitation. Ultimately, surface photovoltage (SPV) experiments prove the enhanced activity of dye-modified PSI even in the solid state.

Modulating semiconductor surface electronic properties by inorganic peptide-binders sequence design.

The use of proteins and peptides as part of biosensors and electronic devices has been the focus of intense research in recent years. However, despite the fact that the interface between the bioorganic molecules and the inorganic matter plays a significant role in determining the properties of such devices, information on the electronic properties of such interfaces is sparse. In this work, we demonstrate that the identity and position of single amino acid in short inorganic binding protein-segments can significantly modulate the electronic properties of semiconductor surfaces on which they are bound. Specifically, we show that the introduction of tyrosine or tryptophan, both possessing an aromatic side chain which higher occupied molecular orbitals are positioned in proximity to the edge of GaAs valence band, to the sequence of a peptide that binds to GaAs (100) results in changes of both the electron affinity and surface potential of the semiconductor. These effects were found to be more pronounced than the effects induced by the same amino acids once bound on the surface in a head-tail configuration. Furthermore, the relative magnitude of each effect was found to depend on the position of the modification in the sequence. This sequence dependent behavior is induced both indirectly by changes in the peptide surface coverage, and directly, probably, due to changes in the orientation and proximity of the tyrosine/tryptophan side group with respect to the surface due to the preferred conformation the peptide adopts on the surface. These studies reveal that despite the use of short protein oligomers and aiming at a non-natural-electronic task, the well-known relations between the proteins' structure and function is preserved. Combining the ability to tune the electronic properties at the interface with the ability to direct the growth of inorganic materials makes peptides promising building blocks for the construction of novel hybrid electronic devices and biosensors.

Self-assembly and self-replication of short amphiphilic ß-sheet peptides.

Most self-replicating peptide systems are made of α-helix forming sequences. However, it has been postulated that shorter and simpler peptides may also serve as templates for replication when arranged into well-defined structures. We describe here the design and characterization of new peptides that form soluble ß-sheet aggregates that serve to significantly accelerate their ligation and self-replication. We then discuss the relevance of these phenomena to early molecular evolution, in light of additional functionality associated with ß-sheet assemblies.

Bioassisted multi-nanoparticle patterning using single-layer peptide templates.

Patterning of nanoparticles on solid substrates is one of the main challenges of current nanotechnology applications. The use of organic molecules as templates for the deposition of the nanoparticles makes it possible to utilize simple soft lithography techniques for patterning. Peptides appear to be powerful candidates for this job due to their versatility and design flexibility. In this work, we demonstrate the use of dual-affinity peptides, which bind both to the substrate and to the deposited nanoparticles, as single-layer linkers for the creation of multi-component nanoparticle patterns via microcontact printing processes. Controlled deposition and patterning of gold colloids or carbon nanotubes (CNTs) on silicon oxide surfaces and that of silicon oxide nanoparticles on gold surfaces have been achieved by the use of the corresponding dual-affinity peptides. Furthermore, patterning of both gold colloids and CNTs on a single substrate on predefined locations has been achieved. The suggested generic approach offers great flexibility by allowing binding of any material to a substrate of choice, provided that a peptide binding segment has been engineered for each of the inorganic components. Furthermore, the diversity of possible peptide sequences allows the formation of multi-component patterns, paving the way to fabricating complex functional structures based on peptide templates.

Effects of mutations in de novo designed synthetic amphiphilic ß-sheet peptides on self-assembly of fibrils.

The self-assembly of two similar amphiphilic peptides into fibril structures is described. Molecular dynamic simulations show that both can organize similarly in a monolayer, but in the fibril bilayer, one prefers a single organization while the other forms two conformational variants. This assembly difference correlates well with our experimental results.

Transient fibril structures facilitating nonenzymatic self-replication.

An emerging new direction of research focuses on developing "self-synthesizing materials", those supramolecular structures that can promote their own formation by accelerating the synthesis of building blocks and/or an entire assembly. It was postulated recently that practical design of such systems can benefit from the ability to control the assembly of amphiphilic molecules into nanostructures. We describe here the self-assembly pathway of short amphiphilic peptides into various forms of soluble ß-sheet structures--ß-plates, fibrils, and hollow nanotubes--and their consequent activity as autocatalysts for the synthesis of monomeric peptides from simpler building blocks. A detailed kinetic analysis of both the self-assembly and self-replication processes allows us to suggest a full model and simulate the replication process, revealing that only specific structures, primarily fibrils that are stable within the solution for a time shorter than a few hours, can be active as catalysts. Interestingly, we have found that such a process also induces fibril reproduction, in a mechanism very similar to the propagation of prion proteins by transmission of misfolded states.