Peptides to bridge biological-platinum materials interface

Abstract

Peptides with inorganic materials recognition already started to impact a wide range of surface-related technologies ranging from biomonitoring to biomedical areas. Combinatorial biology-based libraries are the initial step in tempting the directed evolution of peptides with specific interactions towards technologically relevant materials. Here, a case study is provided to demonstrate the specific peptide binding and the amino acids residues that play an important role for platinum surface affinity by combining computational as well as genetic engineering tools. Using a phage display technique, septapeptides were identified exhibiting affinity to noble metal platinum, and the amino acid distributions in the identified peptides were analyzed. The analysis of the peptide sequences showed that strong Pt-binding peptides contain positively charged, hydrophilic, and polar residues, and especially enriched in threonine, serine, and glutamine. Under competitive surface-binding conditions, strong Pt-binding peptide motif displayed on phage resulted in high specificity to Pt regions on a Pt-macropatterned glass. Conformational analysis of the strong binder indicates that threonine and serine as well as glutamine are in close contact with the surfaces forming a tripod molecular architecture. The alanine substitution mutagenesis applied at the genomic level to the peptide displayed on the phage revealed threonine and serine substitutions as the critical ones. Understanding the residue-based interactions of the peptide sequences can be utilized to tune the affinity and the specificity of the peptides with the inorganic surfaces, toward making them indispensable molecular tools to control the molecular interactions of biological macromolecules with the material surfaces.

Application of Next Generation Sequencing (NGS) in Phage Displayed Peptide Selection to Support the Identification of Arsenic-Binding Motifs

“…The broader metal binding ability of glutamine was further described for copper [58], whereas Chiera et al could even show a major impact of glutamine residues and its H-bonds on the stability of copper-binding peptides [59]. Glutamine was also described to be involved in the surface binding and structure forming of platinum-binding peptides [60] Furthermore, it is described as being abundant in the coordination spheres of metal ions [61,62]. Mitsui et al discovered the QxQ motif in zinc fingers [63].…”

Deep Directed Evolution of Solid Binding Peptides for Quantitative Big-data Generation

“…Using a unique representation of data and conventional bioinformatics tools, the authors also discovered tiny synthesizers from selected peptides that catalyze solid materials synthesis, e.g., gold, silica, and hydroxyapatite, from ionic precursors. 11,12 The phage display selection procedure for biomacromolecules is well-established. But the technique can achieve even further improvement in selectivity by integrating simple modifications into the biopanning protocol (e.g., counter-selection step, material specificity testing, etc.)…”

“…2,7,13,14 Detailed procedures, therefore, are developed for a particular inorganic material in the powder, thin-film, or in single crystal forms and are demonstrated in numerous publications. 9,12,[15][16][17] The selected number of peptides has conventionally been small in the literature, up to a few tens of SBPs. 9,15 The authors ensure that in any SBP-selection, the number of GEPI identified for a given material (either used as a single crystal or a powdered form) are at least 35 (with an average of 50, max 96 peptides).…”

Direct bioelectrocatalysis at the interfaces by genetically engineered dehydrogenase

“…3,4,7,12 Among nature's indispensable repertoire, enzymes, due to their exquisite catalytic features, are certainly one of the most appealing candidates to be utilised as an internal component in next-generation devices. 9,12,14 However, their spatial distribution with the desired orientation on the solid surfaces, operational stability and long-term reuse are among the critical parameters that limit their wide-range integration to functional materials. 2,[10][11][12][13][14][15] There is an urge to develop biological surface functionalisation approaches that will give the ability to control the desired functions at the bio-nanomaterial interfaces with tunability over a multitude of scales.…”