Screening of bacteria-binding peptides and one-pot ZnO surface modification for bacterial cell entrapment.

Masayoshi Tanaka,Ilva Hanun Harlisa,Natasha Agustin Ikhsan,Yuta Takahashi,Mina Okochi

doi:10.1039/c7ra12302g

Masayoshi Tanaka, Ilva Hanun Harlisa + Show 3 more

Open Access

https://doi.org/10.1039/c7ra12302g

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Abstract

Short functional peptides are promising materials for use as targeting recognition probes. Toll-like receptor 4 (TLR4) plays an essential role in pathogen recognition and in activation of innate immunity. Here, the TLR4 amino acid sequence was used to screen for bacterial cell binding peptides using a peptide array. Several octamer peptides, including GRHIFWRR, demonstrated binding to Escherichia coli as well as lipopolysaccharides. Linking this peptide with the ZnO-binding peptide HKVAPR, creates a bi-functional peptide capable of one-step ZnO surface modification for bacterial cell entrapment. Ten-fold increase in entrapment of E. coli was observed using the bi-functional peptide. The screened peptides and the simple strategy for nanomaterial surface functionalization can be employed for various biotechnological applications including bacterial cell entrapment onto ZnO surfaces.

Highlights

The introduction of desired properties onto material surfaces is one of the most important techniques for realizing various bionanotechnological applications
Array-based screening using the amino acid sequence of Toll-like receptor 4 (TLR4) To screen for bacteria-binding peptides, an 8-mer peptide library derived from the 839 amino acid sequence of human
GRHIFWRRLRKALL was capable of binding to the bacterial cell, even though the peptide was in the cytoplasmic region

Summary

Introduction

The introduction of desired properties onto material surfaces is one of the most important techniques for realizing various bionanotechnological applications. Amino acids with carboxylate groups bind preferentially to titanium and silicon owing to their strong electrostatic interactions with the charged surface.[1,2] The strong interaction between gold surfaces and tryptophan is considered to be derived from the planar structure of the amino acid with p-electron bonds characterizing its aromatic ring.[3,4,5] Various peptides with these unique characteristics enabling them to bind to speci c materials are used as non-covalently bound linkers for material surface modi cation.[6,7]. The SPOT-synthesis technique, a method for customized peptide synthesis on a cellulose membrane established by Frank,[13] has been adopted for the screening of functional peptides.[14,15] In particular, the technique is useful for identifying the active site in functional proteins, owing to self-de ned peptide library construction.[16,17]

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