Anchor Peptide-Mediated Surface Immobilization of a Grubbs

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Anchor Peptide-Mediated Surface Immobilization of a GrubbsHoveyda Type Catalyst for Ring-Opening Metathesis Polymerization Alexander R. Grimm, Daniel F. Sauer, Tayebeh Mirzaei Garakani, Kristin Rübsam, Tino Polen, Mehdi D. Davari, Felix Jakob, Johannes Schiffels, Jun Okuda, and Ulrich Schwaneberg Bioconjugate Chem., Just Accepted Manuscript • DOI: 10.1021/acs.bioconjchem.8b00874 • Publication Date (Web): 15 Jan 2019 Downloaded from http://pubs.acs.org on January 20, 2019

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Bioconjugate Chemistry

Title Anchor Peptide-Mediated Surface Immobilization of a Grubbs-Hoveyda Type Catalyst for Ring-Opening Metathesis Polymerization Alexander R. Grimm 1,#, Daniel F. Sauer 1,#, Tayebeh Mirzaei Garakani 1, Kristin Rübsam 1,4, Tino Polen 2, Mehdi D. Davari 1, Felix Jakob 1,4,Johannes Schiffels 1, Jun Okuda 3 and Ulrich Schwaneberg 1,4* Institute of Biotechnology, RWTH Aachen University, Worringer Weg 3, D-52074 Aachen, Germany; IBG-1: Biotechnology, Institute of Bio- and Geosciences, Forschungszentrum Jülich GmbH, D-52425 Jülich, Germany; 3 Institute of Inorganic Chemistry, RWTH Aachen University, Landoltweg 1, D-52056 Aachen, Germany; 4 DWI - Leibniz-Institute for Interactive Materials, Forckenbeckstrasse 50, D-52074 Aachen, Germany * Correspondence: [email protected]; Tel.: +49-241-80-24170 # These authors contributed equally to this work. 1 2

Abstract: Adhesion promoting peptides have been reported to enable efficient enzyme immobilization on various material surfaces. Here we report the first immobilization of a synthetic Grubbs-Hoveyda (GH) type catalyst on two different materials (silica and polypropylene). To this end, the GH catalyst was coupled to an engineered (F16C) variant of the adhesion promoting peptide LCI through thiol-maleimide “click” reaction. Immobilization was performed in an oriented manner through the adhesion promoting peptide by simple incubation with the materials in water and subsequent washing with water and tetrahydrofuran. The immobilized GH catalyst was probed in ring-opening metathesis polymerization of a norbornene derivative to alter the surface properties in a layer-by-layer fashion.

Introduction Balancing hydrophilicity and hydrophobicity of material surfaces is often important for their use in applications 1. Conventional surface modiﬁcation techniques such as selfassembling monolayers (SAMs, e.g. reactions of thiols and metals 2) and organosilane chemistry (e.g. reactions of trichlorosilanes and hydroxyl groups 2) can be applied to compatible materials that e.g. present the necessary functional groups 2-5. For materials lacking functional surface groups such as polypropylene, alternative functionalization strategies are required 6. The challenge in surface modification of polymeric materials is not to alter the bulk properties during the process. Therefore, high temperatures or harsh conditions (e.g. strong acids or bases) cannot be applied. Common strategies to modify surfaces of polymeric materials are e.g. wet chemical treatment of the surface to introduce functional groups (mostly oxygen-containing groups), plasma treatment or UV irradiation. 7 However, these methods are unspecific and affect the layer below the surface-exposed one. Furthermore, already introduced functionalities might be altered by the strategies mentioned above.

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A milder approach is offered by adhesion promoting peptides, also denoted anchor peptides (AP). These APs interact with many surfaces including stainless steel and polymeric surfaces. In contrast to the methods mentioned above, APs are simply deposited on a surface by dipcoating or spraying of a solution containing the AP at room temperature. The interaction with the surface have been proposed via multiple non-covalent interactions (e.g. electrostatic, polar, hydrophobic and hydrogen bonds) as summarized by Seker et al. 8 and Care et al. 9. Since the adsorption behavior of APs is dictated by the amino acid sequence 10, the number of potential surface interactions is limited by the number of residues involved in the interaction 8, 11-12. Increasing the length of the AP has been shown to improve surface binding affinity 13-14. To access a higher diversity in surface interactions, larger APs (up to 100 amino acids) 15 can be used for the functionalization of synthetic polymers (e.g. polymersomes 16-17, polypropylene 12 and polystyrene 18). APs have naturally evolved to interact with biological polymers such as phospholipids and are therefore promising targets to bind to synthetic polymers as well 12, 19. Rübsam et al. employed the ca. 5.5 kDa, positively charged (pI: 10.25) β-stranded anchor peptide LCI from Bacillus subtilis (“liquid chromatography peak I”; PDB ID: 2B9K 20) for polypropylene (PP) binding and achieved a coating density of 0.8 pmol/cm2 12, 20-21. We herein report the first application of an AP for the immobilization of a synthetic organometallic catalyst. Previous reports showed the AP-mediated synthesis of metal nanoparticles 8-9. However, immobilized and defined organometallic catalysts keep their potential control over selectivity that is possible with the organic ligand framework that coordinates the metal ion. The immobilization of a homogeneous catalyst also offers a solution to the important challenge of removing trace metal impurities from pharmaceutical products (maximum acceptable concentration of 10 ppm metal from Rh or Ru catalysts for oral uptake (European Medicines Agency, Doc. Ref. EMEA/CHMP/SWP/4446/2000)) 22-25. As a proof of concept, Grubbs-Hoveyda type catalyst 1 (GH1) anchored to LCI (GH1@LCI) was immobilized on two different surfaces (silica and polypropylene) and used to coat the respective materials with a norbornene polymer film via ring-opening metathesis polymerization (ROMP) 26. Grubbs-Hoveyda type catalysts have been immobilized by chemical means using solid support systems such as polystyrene particles, polyethylene glycol (PEG) resin or sol-gel glass 27-29. However, chemical deposition of metal catalysts cannot be achieved on all surfaces. Moreover, this strategy usually requires a sophisticated ligand design and the orientation of the catalyst is challenging. A more versatile method for the immobilization of synthetic catalysts can be applied by utilizing LCI-based APs. This approach is applicable to a wide variety of maleimide-bearing synthetic catalysts as well as a wide variety of solid supports. By simply drop-casting the coupled GH1@LCI solution on the target material at room temperature, functionalization was achieved in a facile manner. Subsequent ROMP catalysis was selected as a model reaction offering the potential to change the surface properties in a layer-by-layer fashion. Results and Discussion SDS-PAGE was performed to validate the purity of the employed recombinant LCI variants. Fluorescence spectroscopy was used to confirm the functionality of the thiolmaleimide coupling strategy. MALDI-ToF-MS confirmed successful coupling of the GrubbsHoveyda type catalyst (GH1) to the LCI variant. As a model reaction, ring-opening metathesis polymerization (ROMP) of oxanorbornene derivative 1 was performed. Formation of the norbornene polymer via ROMP was confirmed via nuclear magnetic resonance (NMR) spectroscopy and gel permeation chromatography (GPC). Immobilization on polypropylene and silica surfaces was characterized via contact angle measurements and atomic force microscopy (AFM).


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To establish an LCI-based immobilization platform for synthetic catalysts, the first step was the introduction of a cysteine residue within LCI to enable covalent anchoring of the maleimide-bearing synthetic catalyst via thiol-maleimide “click” reaction. For this purpose, a model for surface-adsorbed LCI was built based on the solution structure of LCI (PDB ID: 2B9K 12, 20), and position F16 was selected to provide unobstructed substrate access and to orient the synthetic catalyst away from the surface binding area of LCI (Figure 1). As demonstrated in a previous study 21 and by performing site saturation mutagenesis (SSM) at position 16, the selected position exhibits no significant influence on surface binding (results not shown) and is therefore beneficial for anchoring the metal catalyst.

Figure 1. GH1@LCI_F16C biohybrid catalyst. (a) Conjugation reaction of GH1 to LCI_F16C; (b) Structure of GH1@LCI_F16C. Based on NMR solution structure of wild type LCI (PDB ID: 2B9K). Orange sphere represents Strep-tag-17x helix-TEV cleavage site construct. The structure was generated and visualized with the YASARA software package 30.

The employed LCI_F16C construct consisted of a Strep-tag, 17x-helix spacer to ensure no interactions of the domains, a TEV protease cleavage site and substitution F16C (calculated molecular weight: 9824 g/mol). The construct LCI_F16C was obtained without visible protein contaminants (Figure 2a). In addition to a band at 10 kDa, peptide dimers were observed. Due to the lack of a dimer band for wtLCI, the dimer formation is attributed to disulfide bond formation between the cysteines on LCI_F16C. To ensure accessibility of the thiol group on LCI_F16C, DTT was added as a reductant and subsequently removed by using a desalting column (Figure 2b).


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Figure 2. Purified LCI_F16C and wtLCI analyzed by non-reducing SDS-PAGE. (a) Two LCI_F16C batches and wtLCI after Strep-tag purification, without reducing agents; (b) Three LCI_F16C batches after Strep-tag purification and 1 h incubation with 13 mM DTT at room temperature.

The functionality of the thiol coupling strategy was confirmed using the maleimide-bearing fluorescence indicator ThioGlo®-1, which only exhibits fluorescence upon coupling to thiol groups. ThioGlo®-1 was supplemented to both LCI_F16C and wild type LCI (wtLCI, as a negative control without cysteine). Fluorescence measurements with and without ThioGlo®-1 in a Tecan Infinite M200 96-well plate reader showed low background fluorescence for all samples without ThioGlo®-1 (Figure 3a).

Figure 3. Coupling of fluorescence indicator ThioGlo®-1 to LCI in solution. (a) Fluorescence measurements before (red) and after (blue) incubation of 10 µM LCI variants with 3 eq ThioGlo®-1, which only exhibits fluorescence upon thiol coupling. NaPi buffer was used as a control; (b) Supplementation of 27 µM ThioGlo®-1 to 20 µM LCI_F16C before (left) and after (right) coupling with GH1 catalyst, which prevents ThioGlo®-1 from binding and exhibiting fluorescence.

Upon incubation with ThioGlo®-1 for 10 min, wtLCI showed no substantially increased fluorescence compared to the NaPi buffer control. By contrast, the fluorescence of the LCI_F16C sample incubated with ThioGlo®-1 was substantially increased, reaching RFU values 10-fold higher than the wtLCI negative control, thereby confirming the successful thiolmaleimide coupling. The ThioGlo®-1 setup was subsequently used to determine the coupling efficiency of GH1 to LCI_F16C (Figure 3b). In comparison to the LCI_F16C sample bearing a free thiol group, the GH1@LCI_F16C sample exhibited a 4.5-fold decreased fluorescence, which translates to a coupling efficiency of approx. 78%. Successful generation of the GH1@LCI_F16C biohybrid catalyst was further confirmed via MALDI-ToF-MS analysis (Figure S1). For LCI_F16C with no catalyst attached, a peak at 9812 m/z was observed. This peak corresponds well to the calculated mass for LCI_F16C lacking the GH1 catalyst (9824 ACS Paragon Plus Environment

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g/mol). Upon conjugation, the peak for the apo-protein vanished in the MALDI-ToF-MS spectrum. A new set of peaks appeared that was assigned to the conjugated catalyst and the fragments resulting from the ionization process (Figure S1, black lines). Structural integrity of LCI_F16C after conjugation of GH1 was confirmed via CD spectroscopy (Figure S2). (a)

Incubation 1h

Silica or PP

(b) O

OMe OMe

O

1

OMe OMe

OMe OMe

n

ROMP O

Neat substrate

OMe OMe

O

O

O

n

2OMeOMeOMe OMe

Silica or PP

Figure 4. Schematic depiction of LCI-based surface functionalization procedure. (a) Immobilization of GH1@LCI_F16C on silica or polypropylene (PP); (b) Ring-opening metathesis polymerization of oxanorbornene derivative 1 by immobilized GH1@LCI_F16C.

Next, immobilization of the biohybrid catalyst on a solid support was performed. Since LCI was previously reported to bind to polypropylene (PP) 12, the latter material was used first to immobilize the GH1@LCI_F16C biohybrid catalyst via drop-casting. Chips (1x1 cm, experimental details see below) consisting of PP were rinsed with water and dried under nitrogen (Figure 4a). Next, the chips were incubated with a drop (8 µL) of neat oxanorbornene derivative 1 and incubated for 12 hours (Figure 4b). After reaction time indicated, the chip was sequentially rinsed with water, THF and water and dried under air. Formation of a matt polymer layer on silica was clearly observed visually during the 12 h reaction time. Subsequent NMR and GPC analysis confirmed that the observed film consisted of polymer 2 (Mn = 340,000 g/mol; Figure S3). To evaluate coverage of the PP surface during the different steps of functionalization, contact angle measurements of 1) bare PP (Figure 5a, 113°), 2) after immobilization of LCI_F16C (Figure 5b, 48°), and finally 3) after formation of the polyoxanorbornene film (Figure 5c, 91°) were performed. PP itself is a comparably hydrophobic polymer, as reflected by a contact angle of 113°. Upon drop-casting of the LCI_F16C solution, the contact angle decreased the as expected to 48°. This is explained by the relative hydrophilicity of the LCI_F16C peptide, indicating effective surface coverage. The formation of the moderately water-soluble polyoxanorbornene film was subsequently recorded by an increase in contact angle to ca. 90°.


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Figure 5. Contact angle measurements of ddH2O on polypropylene and silica. (a) Bare polypropylene (PP); (b) LCI_F16C immobilized on PP; (c) Polyoxanorbornene 6 layer on PP after immobilization of GH1@LCI_F16C; (d) Bare silica; (e) LCI_F16C immobilized on silica; (f) Polyoxanorbornene 6 layer on silica after immobilization of GH1@LCI_F16C.

In addition to PP, silica was also successfully functionalized, as confirmed by contact angle measurements (Figure 5d-f). While contact angles for bare PP and silica differed significantly (113° and 59°, respectively), upon immobilization of LCI_F16C, contact angles became remarkably similar (48° and 40°, respectively). After formation of the polyoxanorbornene film, a contact angle of 88° was measured, which is virtually the same value as determined for PP, indicating that similar surface coverage was achieved in both cases, independently of the employed solid support. Utilizing silica as a solid surface also enabled the determination of deposited GH1@LCI_F16C film thickness via AFM. After scratching the GH1@LCI_F16C layer on the silica chip, AFM analysis supported contact angle measurements by showing a densely packed GH1@LCI_F16C film (Figure 6a).

Figure 6. Atomic force microscopy (AFM) measurements of GH1@LCI_F16C immobilized to silica chip. (a) AFM images of cut surface; (b) Height profile of cut section.


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Inspection of the height profile revealed a height difference of 2-3 nm on average between the bare silica and GH1@LCI_F16C coated area (Figure 6b), indicating the formation of a GH1@LCI_F16C monolayer on the silica surface. In comparison, a previously immobilized LCI-eGFP fusion protein film reportedly had a thickness of 4-5 nm 12. Conclusions In summary, a synthetic metal catalyst was immobilized on two different solid supports (silica and PP) utilizing the LCI_F16C anchor peptide for GH catalyst immobilization for the first time. Catalytic activity was confirmed by polymerizing an oxanorbornene derivative. The resulting polymerfilm fully covered the solid support as indicated by a change in the resulting contact angle (from ca. 40° to 90°). The developed immobilization strategy enables a layer-bylayer film formation with a nm-size thickness. The immobilization efficiency (monolayer deposition) and simplicity in application render the technology generally applicable for a broad range of materials. This opens routes towards novel opportunities through immobilization of homogeneous catalysts, e.g. in cascade or tandem reactions. Furthermore, the spatial separation of the metal sites on the surface avoids agglomeration of the catalysts even in neat substrates. Additionally, through immobilization of the homogeneous catalysts, the separation of formed products and catalysts is facilitated, which remains a significant challenge e.g. in the pharmaceutical industry. Materials and Methods Reagents and Devices All buffer components were obtained from AppliChem. Circular dichroism (CD) spectra were obtained with a JASCO J1100 spectrometer. pH values were measured with a Horiba F52 pH meter. Fluorescence measurements were performed with a Tecan Infinite M200 96-well plate reader. MALDI–TOF MS spectra were recorded on an Ultraflex III TOF/TOF mass spectrometer from Bruker using 2,5-dihydroxybenzoic acid (DHB) as matrix. All chemical experiments were performed under nitrogen atmosphere using standard Schlenk techniques or a MBraun nitrogen-filled glovebox. THF was degassed by using “pumpfreeze-thaw” cycles. 1H NMR spectra were obtained with a Bruker Avance III 400 NMR spectrometer. Chemical shifts are reported in ppm relative to the residual solvent resonances 31. Gel permeation chromatography (GPC) was measured on an Agilent Series 1100 (Midland, ON, Canada), equipped with two SDV linear N columns of 8×300 mm and 8×600 mm measures and 5 μm pore size, in THF at 30 °C against a poly(styrene) standard. Grubbs-Hoveyda type complex GH1 32 and substrate 1 33 were synthesized as previously reported. Amino Acid Sequence of LCI_F16C Construct The amino acid sequence of the employed LCI_F16C construct is given below (N-terminal strep-tag, 17x helix spacer, TEV protease cleavage site, LCI_F16C): WSHPQFEKAEAAAKEAAAKEAAAKAENLYFQGAIKLVQSPNGNFAASCVLDGT KWIFKSKYYDSSKGYWVGIYEVWDRK Immobilization Procedure Preparation of Silica and Polypropylene Samples Silica wafers and polypropylene (PP) blocks (now termed “chips”) were cut into 1 cm x 1 cm squares, then rinsed with ddH2O. After drying with N2, the chips consisting of silica and PP were incubated in toluene and pentane, respectively, overnight to remove impurities. Silica and ACS Paragon Plus Environment

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PP chips were subsequently dried at air, then ultrasonicated in acetone and ethanol, respectively, for 20 min. This was followed by a second ultrasonication step in ddH2O for another 20 min. After a final rinsing step with ddH2O and drying with N2, the silica and PP surfaces were ready for use. Immobilization of LCI_F16C on Silica and Polypropylene For the deposition of LCI_F16C without the GH1 catalyst, purified LCI_F16C was incubated with 13 mM DTT for 1 h at room temperature. Following a buffer exchange to 50 mM Tris/Cl, pH 8 using a HiTrap desalting column, 200 µl of 10 µM LCI_F16C solution was pipetted on silica or PP surfaces and incubated for 1 h. Excess LCI was then removed by washing with 50 mM Tris/Cl buffer (pH 8). The LCI-covered samples were finally dried under N2. Grubbs-Hoveyda type Catalyst GH1 Coupling and Immobilization For the immobilization of GH1@LCI_F16C, GH1 was first coupled to LCI_F16C in solution. Subsequently, 200 µl of 10 µM coupled GH1@LCI_F16C was then pipetted on silica or PP surfaces and incubated for 1 h. Excess GH1@LCI_F16C was removed by washing with 50 mM Tris/Cl buffer (pH 8) followed by ddH2O. The GH1@LCI_F16C-covered samples were finally dried in the N2-Glovebox. Ring-Opening Metathesis Polymerization For ROMP of oxanorbornene derivative 1 mediated by immobilized GH1@LCI_F16C, a 8 µl drop of oxanorbornene 1 was placed on either silica or PP pretreated with the biohybrid catalyst to cover the entire sample surface, and incubated for 12 h at room temperature. After polymer film formation, the samples were extensively washed with ddH2O, THF and lastly ddH2O. For 1H-NMR and GPC analysis, the plate was incubated with 100 µL ethyl vinyl ether for 1 h to quench the Grubbs-Hoveyda type catalyst and to cleave the polymer from the surface. The mixture was dried in a N2 stream and the residue was dissolved in CDCl3 for 1H-NMR analysis according to Feast and Harrison34 or in THF for GPC-Analysis, respectively (supporting information figure S3).

Associated Content Supporting Information: The Supporting Information is available free of charge on the ACS Publication website at DOI: Figure S1: MALDI-ToF-MS results of LCI_F16C (red) and GH3@LCI_F16C (black), Figure S2: Circular dichroism (CD) curves of LCI_F16C (black) and GH1@LCI_F16C (red), Figure S3: Polymer analysis. Author Information Corresponding Author *E-mail: [email protected] Author Contributions #Alexander

R. Grimm und Daniel F. Sauer contributed equally to this work. ACS Paragon Plus Environment

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Notes The authors declare no competing financial interest.

Acknowledgments: This research was financially supported by the Deutsche Forschungsgemeinschaft (DFG) through the International Research Training Group “Selectivity in Chemo- and Biocatalysis” (SeleCa) and the Bundesministerium für Bildung und Forschung (BMBF) (FKZ: 031B0297). Umicore, Frankfurt (Dr. A. Doppiu) is gratefully acknowledged for a generous gift of ruthenium precursor. References 1. Penn, L.; Wang, H., Chemical modification of polymer surfaces: a review. Polym. Adv. Technol. 1994, 5 (12), 809-817. 2. Vos, J. G.; Forster, R. J.; Keyes, T. E., Interfacial supramolecular assemblies. John Wiley & Sons: 2003. 3. Love, J. C.; Estroff, L. A.; Kriebel, J. K.; Nuzzo, R. G.; Whitesides, G. M., Selfassembled monolayers of thiolates on metals as a form of nanotechnology. Chem. Rev. 2005, 105 (4), 1103-1170. 4. Ulman, A., Formation and Structure of Self-Assembled Monolayers. Chem. Rev. 1996, 96 (4), 1533-1554. 5. Metzke, M.; Bai, J. Z.; Guan, Z., A novel carbohydrate-derived side-chain polyether with excellent protein resistance. J. Am. Chem. Soc. 2003, 125 (26), 7760-7761. 6. Kang, S. M.; Rho, J.; Choi, I. S.; Messersmith, P. B.; Lee, H., Norepinephrine: MaterialIndependent, Multifunctional Surface Modification Reagent. J. Am. Chem. Soc. 2009, 131 (37), 13224-13225. 7. Goddard, J. M.; Hotchkiss, J. H., Polymer surface modification for the attachment of bioactive compounds. Prog. Polym. Sci. 2007, 32 (7), 698-725. 8. Seker, U. O. S.; Demir, H. V., Material binding peptides for nanotechnology. Molecules 2011, 16 (2), 1426-1451. 9. Care, A.; Bergquist, P. L.; Sunna, A., Solid-binding peptides: smart tools for nanobiotechnology. Trends Biotechnol. 2015, 33 (5), 259-268. 10. Kuang, Z.; Kim, S. N.; Crookes-Goodson, W. J.; Farmer, B. L.; Naik, R. R., Biomimetic chemosensor: designing peptide recognition elements for surface functionalization of carbon nanotube field effect transistors. ACS Nano 2009, 4 (1), 452-458. 11. Kriplani, U.; Kay, B. K., Selecting peptides for use in nanoscale materials using phagedisplayed combinatorial peptide libraries. Curr. Opin. Biotechnol. 2005, 16 (4), 470-475. 12. Rübsam, K.; Stomps, B.; Böker, A.; Jakob, F.; Schwaneberg, U., Anchor peptides: A green and versatile method for polypropylene functionalization. Polymer 2017, 116, 124-132. 13. Serizawa, T.; Techawanitchai, P.; Matsuno, H., Isolation of peptides that can recognize syndiotactic polystyrene. ChemBioChem 2007, 8 (9), 989-993. 14. Kacar, T.; Zin, M. T.; So, C.; Wilson, B.; Ma, H.; Gul‐Karaguler, N.; Jen, A. K. Y.; Sarikaya, M.; Tamerler, C., Directed self‐immobilization of alkaline phosphatase on micro‐patterned substrates via genetically fused metal‐binding peptide. Biotechnol. Bioeng. 2009, 103 (4), 696-705. 15. Wang, Z.; Wang, G., APD: the antimicrobial peptide database. Nucleic Acids Res. 2004, 32 (suppl_1), D590-D592. 16. Noor, M.; Dworeck, T.; Schenk, A.; Shinde, P.; Fioroni, M.; Schwaneberg, U., Polymersome surface decoration by an EGFP fusion protein employing Cecropin A as peptide “anchor”. J. Biotechnol. 2012, 157 (1), 31-37. ACS Paragon Plus Environment

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TOC-Graphic Silica

Silica + LCI_F16C

Silica + LCI + Oxanorbornene

OMe OMe

O

OMe OMe


O

OMe OMe

O

O

n

OMe OMe

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Anchor Peptide-Mediated Surface Immobilization of a Grubbs

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