Selection of peptides binding to metallic borides by screening M13 phage display libraries

Abstract

BackgroundMetal borides are a class of inorganic solids that is much less known and investigated than for example metal oxides or intermetallics. At the same time it is a highly versatile and interesting class of compounds in terms of physical and chemical properties, like semiconductivity, ferromagnetism, or catalytic activity. This makes these substances attractive for the generation of new materials. Very little is known about the interaction between organic materials and borides. To generate nanostructured and composite materials which consist of metal borides and organic modifiers it is necessary to develop new synthetic strategies. Phage peptide display libraries are commonly used to select peptides that bind specifically to metals, metal oxides, and semiconductors. Further, these binding peptides can serve as templates to control the nucleation and growth of inorganic nanoparticles. Additionally, the combination of two different binding motifs into a single bifunctional phage could be useful for the generation of new composite materials.ResultsIn this study, we have identified a unique set of sequences that bind to amorphous and crystalline nickel boride (Ni3B) nanoparticles, from a random peptide library using the phage display technique. Using this technique, strong binders were identified that are selective for nickel boride. Sequence analysis of the peptides revealed that the sequences exhibit similar, yet subtle different patterns of amino acid usage. Although a predominant binding motif was not observed, certain charged amino acids emerged as essential in specific binding to both substrates. The 7-mer peptide sequence LGFREKE, isolated on amorphous Ni3B emerged as the best binder for both substrates. Fluorescence microscopy and atomic force microscopy confirmed the specific binding affinity of LGFREKE expressing phage to amorphous and crystalline Ni3B nanoparticles.ConclusionsThis study is, to our knowledge, the first to identify peptides that bind specifically to amorphous and to crystalline Ni3B nanoparticles. We think that the identified strong binding sequences described here could potentially serve for the utilisation of M13 phage as a viable alternative to other methods to create tailor-made boride composite materials or new catalytic surfaces by a biologically driven nano-assembly synthesis and structuring.

Exploring the Secretomes of Microbes and Microbial Communities Using Filamentous Phage Display

“…Biopanning has potential to identify proteins that bind to enormous diversity of ligands, from extremely complex, including the whole animal ( Arap et al, 1998 ), ex vivo tissues ( Antonara et al, 2007 ), complex mixture of organisms ( Ng F. et al, 2015 ) and whole cells ( Fevre et al, 2014 ) to very simple, such as purified proteins, peptides, nucleic acids, carbohydrates ( Zwick et al, 1998 ; Rodi and Makowski, 1999 ) or inorganic powders ( Mao et al, 2004 ; Ploss et al, 2014 ). The outcome of biopanning, however, depends on library complexity (or primary size, equivalent to the number of different variants or recombinant inserts), functionality of displayed fusions and affinity of interaction with the bait used in the biopanning.…”

Biogenic and Synthetic Peptides with Oppositely Charged Amino Acids as Binding Sites for Mineralization

“…A seven-mer inorganic-binding peptide (LGFREKE) which was identified as strongest interacting peptide for amorphous and crystalline nickel boride (Ni 3 B) contained two duplet motifs in its sequence [25]. …”

“…In addition, for other inorganic-binding peptides interacting with Pd [ 22 ], Pt [ 22 , 23 ], Ag [ 24 ] a duplet motif in the peptide sequence is present. A seven-mer inorganic-binding peptide (LGFREKE) which was identified as strongest interacting peptide for amorphous and crystalline nickel boride (Ni 3 B) contained two duplet motifs in its sequence [ 25 ].…”

Phage-Displayed Peptides Selected to Bind Envelope Glycoprotein Show Antiviral Activity against Dengue Virus Serotype 2

“…Some of the binding phages shown here carried peptide sequences already reported at the biopanning data bank, a repository that, at the moment of writing this paper, had more than 23,700 sequences appearing in biopanning data [ 36 ]. The peptides SPSTHWK and WNAKYTL were also previously reported to bind crystalline Ni3B nanoparticles [ 37 ]. Also, the peptide NERALTL appeared twice in the database, with binding activity to epoxy covered surfaces [ 38 ] and to the fusion protein of the infectious salmon anemia virus [ 39 ].…”