Discovery of Catalytic Peptides for Inorganic Nanocrystal Synthesis by a Combinatorial Phage Display Approach

Wei, Zengyan; Maeda, Yoshiaki; Matsui, Hiroshi

doi:10.1002/anie.201102582

Cited by 24 publications

(17 citation statements)

References 30 publications

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“…In this study, the same clones showing multiple appearances, namely, Pd‐1, Pd‐2, and Pd‐3, were investigated. However, it should be noted that the affinity of phage clones to the target samples is not always necessarily proportional to the frequency of appearance, probably due to unfavorable virus amplification during biopanning 7a,11b,12. To quantify the adsorption behavior of the selected phage clones to Pd NPs, ELISA was performed.…”

Section: Resultsmentioning

confidence: 99%

“…As shown in Figure 4, the bound amount of Pd‐1 peptide is 920 ng/cm 2 , which is much greater than that in the control experiment, 130 ng/cm 2 . A small number of the control peptides are still bound to the substrate; this could be due to nonspecific adsorption 7a,12. This result suggests that, even without the virus body, the Pd‐1 peptide shows strong affinity to the {100} facets of Pd.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Insights into the Bioactivity of Mensacarcin and Epoxide Formation by MsnO8

Maier¹,

Pflüger²,

Loesgen³

et al. 2014

ChemBioChem

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Mensacarcin, a potential antitumour drug, is produced by Streptomyces bottropensis. The structure consists of a three-membered ring system with many oxygen atoms. Of vital importance in this context is an epoxy moiety in the side chain of mensacarcin. Our studies with different mensacarcin derivatives have demonstrated that this epoxy group is primarily responsible for the cytotoxic effect of mensacarcin. In order to obtain further information about this epoxy moiety, inactivation experiments in the gene cluster were carried out to identify the epoxy-forming enzyme. Therefore the cosmid cos2, which covers almost the complete type II polyketide synthase (PKS) gene cluster, was heterologously expressed in Streptomyces albus. This led to production of didesmethylmensacarcin, due to the fact that methyltransferase genes are missing in the cosmid. Further gene inactivation experiments on this cosmid showed that MsnO8, a luciferase-like monooxygenase, introduces the epoxy group at the end of the biosynthesis of mensacarcin. In addition, the protein MsnO8 was purified, and its crystal structure was determined to a resolution of 1.80 Å.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Insights into the Bioactivity of Mensacarcin and Epoxide Formation by MsnO8

Maier¹,

Pflüger²,

Loesgen³

et al. 2014

ChemBioChem

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show abstract

“…The Matsui group (72) developed a novel strategy to isolate catalytic peptides by utilizing the so-called anchor effect of nanocrystals. Figure 2 a highlights the basic strategy of this method, in which ZnO crystallization was used as a proof of concept.…”

Section: Combinatorial Approaches To Identify Catalytic Peptidesmentioning

confidence: 99%

Design of Catalytic Peptides and Proteins Through Rational and Combinatorial Approaches

Maeda

Makhlynets

Matsui

et al. 2016

Annu. Rev. Biomed. Eng.

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This review focuses on recent progress in noncomputational methods to introduce catalytic function into proteins, peptides, and peptide assemblies. We discuss various approaches to creating catalytic activity and classification of noncomputational methods into rational and combinatorial classes. The section on rational design covers recent progress in the development of short peptides and oligomeric peptide assemblies for various natural and unnatural reactions. The section on combinatorial design describes recent advances in the discovery of catalytic peptides. We present the future prospects of these and other new approaches in a broader context, including implications for functional material design.

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“…For such direct screening of the binding event the phage display library has been used extensively; however the direct discovery of catalytic peptides from a combinatory phage display library meets difficulty in the panning process; even though certain peptides from random sequences on phage viruses catalyze target reactions, the isolation of these catalytic peptides for the identification of sequences through gene analysis is very difficult. Previously, peptide catalysts for the room temperature growth of inorganic materials were screened with a combinatory phage display library by directly mixing the library system in precursor solutions, however it is necessary to choose precursors that do not grow any by‐products except target materials, and such a special condition is not generally applicable to screen peptides for a variety of chemical reactions . Recently, a new strategy to discover peptide catalysts for various material syntheses was demonstrated by combining combinatory phage display library and hydrogelation; as the phage display library is introduced in the solution containing aromatic short‐peptide derivatives of gel precursors, the product formation between these peptide derivatives induces gelation around viruses where catalytic peptides are displayed, and these catalytic viruses can be separated by mass.…”

Section: Figurementioning

confidence: 99%

Enzyme‐Mimicking Peptides to Catalytically Grow ZnO Nanocrystals in Non‐Aqueous Environments

et al. 2015

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The application of enzymesf or biomimetic material growth is ap otential path to breakthroughs in catalytic inorganic nanocrystal synthesis because the biocatalytic functions of proteins can lead to highly efficient growth of materials with accurate structures at low temperature. However,m any metal nanocrystals are grown in organic solvents, which is not an ideal environment for biomineralization with enzymes due to denaturing of catalytic pocket structures. Here, we applied ac atalytic CP4 peptide, optimized for protease reactions such as amide and ester hydrolysis, to test the catalytic ZnO nanocrystal growth in non-aqueous environments and the performance was compared with the enzyme subtilisin. We demonstrated that the CP4 catalytic peptide, evolved by the hydrogel-based combinatory phage display library, could grow ZnO nanoparticles from zinc acetate precursors in higher crystallinitya nd yield, as compared to the protease enzyme, in an organics olvent by catalyzing ester-elimination of precursors at room temperature.T his result indicates that catalytic oligopeptides, which possess no rigid 3D structures but are rather flexible, could fold into the catalytically active conformation more frequently in harsh environments such as organic solvents.Complex biomolecular systemss uch as enzymes, viruses, and bacteria have been applied for inorganic nanocrystal synthesis. [1] While these systems could catalyze nanocrystal growth under ambient conditions in aqueous environments, for further diversecatalytic applications it is desirable to optimizetheir activities for tolerating harsh organic environments. Recently, peptides, short building blocks of proteins,h ave shown potential to possesst he catalytic activity for enzymatic reactions in materialg rowth. [2] While some peptides have been shown to exhibit high catalytic activity in chemical reactions and material growth in ambient conditions, [2g] these peptides are not directly discovered to catalyze the target material growth, but they are rather selected on the basis of binding affinity to intermediates and products.F or such direct screening of the binding event the phage displayl ibrary has been used extensively; however the direct discovery of catalytic peptides from ac ombinatory phage display library meets difficultyi nt he panning process;e ven though certain peptides from random sequences on phage viruses catalyze target reactions, the isolation of these catalytic peptides for the identification of sequences through gene analysisi sv ery difficult. Previously,p eptidec atalysts for the room temperature growth of inorganic materials were screened with ac ombinatory phage display library by directly mixingthe library system in precursor solutions, however it is necessary to choose precursors that do not grow anyb yproducts except target materials, and such as pecial condition is not generally applicable to screen peptides for av arietyo f chemicalr eactions. [3] Recently,anew strategy to discover peptide catalysts for various material syntheses was demo...

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Discovery of Catalytic Peptides for Inorganic Nanocrystal Synthesis by a Combinatorial Phage Display Approach

Cited by 24 publications

References 30 publications

Insights into the Bioactivity of Mensacarcin and Epoxide Formation by MsnO8

Insights into the Bioactivity of Mensacarcin and Epoxide Formation by MsnO8

Design of Catalytic Peptides and Proteins Through Rational and Combinatorial Approaches

Enzyme‐Mimicking Peptides to Catalytically Grow ZnO Nanocrystals in Non‐Aqueous Environments

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