Investigation on Adsorption Mechanism of Peptides with Surface

Subscriber access provided by Macquarie University

Interfaces: Adsorption, Reactions, Films, Forces, Measurement Techniques, Charge Transfer, Electrochemistry, Electrocatalysis, Energy Production and Storage

Investigation on Adsorption Mechanism of Peptides with Surface-Modified Super Macroporous Resins Hao Wang, Ruirui Liu, Yongfeng Liu, Yajie Meng, Yi Liu, Honglin Zhai, and Duolong Di Langmuir, Just Accepted Manuscript • DOI: 10.1021/acs.langmuir.8b03997 • Publication Date (Web): 22 Feb 2019 Downloaded from http://pubs.acs.org on February 22, 2019

Just Accepted “Just Accepted” manuscripts have been peer-reviewed and accepted for publication. They are posted online prior to technical editing, formatting for publication and author proofing. The American Chemical Society provides “Just Accepted” as a service to the research community to expedite the dissemination of scientific material as soon as possible after acceptance. “Just Accepted” manuscripts appear in full in PDF format accompanied by an HTML abstract. “Just Accepted” manuscripts have been fully peer reviewed, but should not be considered the official version of record. They are citable by the Digital Object Identifier (DOI®). “Just Accepted” is an optional service offered to authors. Therefore, the “Just Accepted” Web site may not include all articles that will be published in the journal. After a manuscript is technically edited and formatted, it will be removed from the “Just Accepted” Web site and published as an ASAP article. Note that technical editing may introduce minor changes to the manuscript text and/or graphics which could affect content, and all legal disclaimers and ethical guidelines that apply to the journal pertain. ACS cannot be held responsible for errors or consequences arising from the use of information contained in these “Just Accepted” manuscripts.

is published by the American Chemical Society. 1155 Sixteenth Street N.W., Washington, DC 20036 Published by American Chemical Society. Copyright © American Chemical Society. However, no copyright claim is made to original U.S. Government works, or works produced by employees of any Commonwealth realm Crown government in the course of their duties.

Page 1 of 23 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Langmuir

Investigation on Adsorption Mechanism of Peptides with Surface-Modified Super Macroporous Resins

Hao Wang1,2, Ruirui Liu3, Yongfeng Liu1,4, Yajie Meng3, Yi Liu1,4, Honglin Zhai3*, Duolong Di1,4* 1. CAS Key Laboratory of Chemistry of Northwestern Plant Resources, Key Laboratory for Natural Medicine of Gansu Province, Lanzhou Institute of Chemical Physics, Chinese Academy of Sciences, Lanzhou 730000, P. R. China 2. University of Chinese Academy of Sciences, Beijing 100049, P. R. China 3. College of Chemistry & Chemical Engineering, Lanzhou University, Lanzhou, 730000, P. R. China 4. Qingdao Center of Resource Chemistry & New Materials, Qingdao 266071, P. R. China

ABSTRACT: Macroporous adsorption resins (MAR) have experienced rapid growth due to their unique properties and applications. Recently, it was discovered that a series of MAR with super macroporous and diverse functional groups were synthesized to adsorb and enrich peptides; however, the detailed change mechanism of pore diameter and element composition and peptide adsorption mechanism have not yet been established. In this study, MAR and modified MAR were prepared by surfactant reverse micelles swelling method and Friedel–Crafts reaction, and the pore diameter and element changes of these super macroporous resin particles were accurately determined to elucidate formation processes of modified MARs. Four peptides adsorption mechanism on different MARs were investigated. Sieving effect, electrostatic, hydrophobic and hydrogen bonds interactions were found to play a major role in the adsorption process of peptides. Compared to the traditional resins, the adsorption capacity of super macroporous MAR for peptides enormously increased. Electrostatic interactions have been explained perfectly by determining the isoelectric point. The molecular docking technology proved that hydrogen bonding receptor in MAR was a crucial factor for the adsorption capacity by autodock 4.26 and gromacs 5.14. These findings will enable selective adsorption of peptides by MAR, which also provides a theoretical basis for the construction of specific resin to adsorb different peptides. KEYWORDS: Super Macroporous Resins, Peptides Adsorption Mechanism, Surface-Modified, Molecular docking technology

ACS Paragon Plus Environment

Langmuir 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

INTRODUCTION Peptide is a specific bioactive compound between amino acids and proteins, generally speaking, which are divided into endogenous peptides from human and exogenous peptides from other creatures. In cell biology, peptides are usually considered intermediate degradation products on their way to full degradation. Then, free amino acids can be used to build new proteins.1 But in recent decades, because of their relatively safe and well tolerated therapeutic potential, multifaceted immunomodulatory activities and unique biological activity, peptides have been utilized in many fields. Peptides as drugs are increasingly being studied, as they are safer and more selective than small molecule drugs, whose side effects in vivo are extensive. Opioid peptides can bind to gut opioid receptors and alter gastrointestinal motility, and antimicrobial peptides can inhabit pathogen growth.2 Approximately 140 peptide therapeutics are currently being evaluated in clinical trials.3 Antimicrobial peptides have since been found to exhibit multifaceted immunomodulatory activities, for instance anti-infective and selective anti-inflammatory.4 Peptides, owing to their biomolecular recognition potential, offer unique possibilities for the development of efficient and selective fluorescent sensors.5 Peptide can be regarded as targets to investigate food allergen detection by mass spectrometry.6 There are two ways to obtain peptides, directly synthesis or separation and enrichment from nature. At present, peptides synthesis is still the most widely used methods, but there are lots of shortcomings, such as time consuming, high cost and low activity. By comparison, peptide separation and enrichment from nature are more convenient and economical. Of course, with the development of separation technology, many methods, membrane technology,7 gel chromatography,8 ion exchange resins9 and macroporous adsorption resins (MAR),10 can be used peptide separation. Compared to membrane technology, MAR obtain not only sieving effect, but also adsorption effect. Compared to gel chromatography, MAR is more high-speed. As for ion exchange resin, MAR is more low-cost and versatile, because some peptides are easy to lose their activity.11 MAR has been utilized in numerous fields for recent decades. Because of high specific surface areas and remarkable absorption, they can be applied as stationary phases in separation field12, carriers for soild phase organic and peptide synthesis, ion-exchange resins, catalysts,13 scavenging14 and enzyme supports. Taking into account their special application, important parameters of these particles are average pore size, average particle diameter, specific surface area, pore volume, mean effective porosity, particle shape, etc.15 According to the IUPAC defined pore diameters, porous particles are divided into microporous, mesoporous and macroporous structures depending on the size of the pore, 50 nm. In general, the application should be kept in


Page 2 of 23

Page 3 of 23 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Langmuir

mind prior to choosing synthetic technology. As a result, the researchers developed different methods. Suspension,16 precipitation,17 multistage, dispersion19 and microfluidic20 membrane emulsification,18 polymerizations are most commonly used methods. In recent years, small pore size (100 nm), have been obtained.22 At the same time, these particles are also further modified for better separation of macromolecules.22 Many applications require a regularly shaped structure with specific average pore size and distribution. The formation of pores in the particles can be considered as a process of aqueous phase and oil phase separation, either in suspension or in swelling and polymerization.15 The pore size can be indirectly controlled by some factors, for example, the stirring speed in the polymerization process, the reaction temperature, the cross-linking degree, the reaction time, etc.21, 23 Preparation of gigaporous particles have attracted great attention over the past decade, and their pore diameters are generally greater than 100 nm.21,22 The aim of this work was to obtain a series of modified super macroporous MARs to peptide separation and enrichment. Commercial resins modified by these functional groups were investigated in previous studies, but they only focused on the improved adsorption results, while ignored the investigation of structure and adsorption mechanism. We intended to compare the traditional and commercialized MAR and to explain the process of modified material preparation and the mechanism to understand the adsorption in greater detail. MATERIALS AND METHODS Materials. Styrene (St, AR) and Ethylene glycol dimethacrylate (EGDMA, AR) was acquired from Tianjin Damao Chemical Reagent Factory. St and EGDMA were passed through a pad of neutral alumina to removed radical inhibitor prior to use. The initiator benzoyl peroxide (BPO) was purchased from Beijing Chemical Reagents Co. The preparation, characterization, and pore properties of poly(styrene-co-ethylene glycol dimethacrylate) (PSE) in this work were described in our previous work.24 Distilled water was prepared in our laboratory. Chloromethyl methyl ether of pharmaceutical grade was obtained from Jinan Chemical Reagent Co., Inc. Other chemicals were of analytical reagent grade. Sodium chloride, zinc chloride, sodium hydroxide, acetonitrile and dichloromethane were purchased from Tianjin Chemical Reagent Co., Inc. Diethylenetriamine (DETA), N,N-Dimethylformamide (DMF), imidazole (MI), p-phenylene diamine (PPD) and 4-aminobenzoic acid (PAA) were purchased from Sinopharm Chemical Reagent Co., Ltd. Buffer compositions are as follows: citrate buffered saline pH 3 and pH 5, phosphate buffered saline (PBS) ph 7.4,


Langmuir 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

and carbonate buffer saline pH 9.2 and pH 10.7. Glutathione (GSH), bradykinin (BK), insulin (INS) and bovine serum albumin (BSA) were obtained from Amresco. MARs including BSKB-1, BWKX-4, BNKX-5 and Chloromethyl Polystyrene Resins (CMPs) were purchased from Xi’an Sun Resin Technology Co., Ltd. (Shaanxi, China). Synthesis of Adsorbents with Functional Groups. The reaction scheme for the preparation of PSE-Cl, PSE-MI, PSE-PAA, PSE-PPD and PSE-DETA on the basis of PSE is shown in Figure 1. The initial resin particles (PSE) were soaked in tetrachloromethane for 24 h. Zinc chloride, sodium chloride, and PSE were suspended with chloromethyl methyl ether at 311 K for 4 h with mechanical agitation (120 rpm). After the reaction, the particles chloromethyl/PSE (PSE-Cl) were washed with ethanol and subsequently with distilled water before they were dried in a vacuum. PSE-Cl was swollen with acetonitrile overnight and then mixed with imidazole and sodium hydroxide in a 250 ml three-neck, round-bottom flask. The reaction was maintained at 353.15 K for 6 h in a nitrogen atmosphere. After the reaction, the particles imidazole/PSE (PSE-MI) were washed with ethanol and distilled water before they were dried in a vacuum. PSE-Cl, sodium chloride and sodium hydroxide were swollen with DMF overnight and then mixed with PAA, PPD and DETA in three 250 ml three-neck, round-bottom flask, respectively. The flasks were heated with a programmed heater. The mixture was stirred to give a suspension of beads of a suitable size in the solution and then held at 328.15 K for 20 h. The synthetic particles were filtered out, packed in an extractor, and washed with a large amount of distilled water and then methanol until there was no white precipitate while an aqueous solution of silver nitrate was added to the filtrate.

Figure 1. Reaction scheme for the preparation of PSE-Cl, PSE-MI, PSE-PAA, PSE-PPD and PSE-DETA on the basis of PSE.

Characterization. The BET specific surface area, average pore size, and pore volume of the adsorbents were determined by N2


Page 4 of 23

Page 5 of 23 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Langmuir

adsorption/desorption isotherms at 77.15 K using a Micromeritics ASAP 2020 automatic surface area and porosity analyzer (Micromeritics Instrument Corp., Norcross, GA) by the BET method. The particles were outgassed for 24 h with the temperature of BET surface area. The BET surface area was obtained by the t-plot method. Meanwhile, the pore volume and average pore diameter were estimated by the Barrett-Joyner-Halenda (BJH) method. The infrared spectra were obtained using Fourier-transform infrared spectrometry (FTIR) with a spectrophotometer in the 4000-400 cm-1 region via the KBr pellet method. A field-emission scanning electrode microscope (Hitachi SU8020, Japan) was used for the morphological characterization of the particles. X-ray photoelectron spectroscopy (XPS) measurements were carried out on XPS instrument (Escalab 250, Thermo SCIENTIFIC, America). All binding energies were referenced to the C 1s pesks of the surface adventitious carbon at 284.8 eV. Synchronous illumination XPS (SIXPS) was conducted on XPS instrument (Escalab 250Xi, Thermo SCIENTIFIC, America) and a 300 W Xe arc lamp acted as illumination source. The changes of XPS spectra were obtained via controlling light on or off at given time intervals in the process of measurements. Elemental measurements were carried out on Elemental analyzer (Vario EL, Elementer, Germany). The morphologies of samples were characterized with Field Emission Scanning Electron Microscope (S4800, HITACHI, Japan). Peptide Adsorption The nitrogen-containing porous polymer particles (0.1 g) were soaked in ethanol for 3 h, then washed with distilled water to remove leftover ethanol. Biomolecule was used as adsorbate to perform the adsorption experiments. N-particles were conducted with 50 mL sample solution with initial concentrations of 0.5 mg/mL in a 100 mL conical flask. The flask was continuously shaken at 298.15 K. The adsorption time and stirring speed were set at 8 h and 100 rpm, respectively. HPLC Analysis of biomolecules The HPLC analysis was performed in an Agilent 1200 Series (Agilent Technology, Santa Clara, CA), which was equipped with a G1312A binary pump, a G1315B diode array detector and a G1328B manual injector. The HPLC system was managed by Agilent Chemstation software (version A.10.02) (Agilent Technology). The standards GSH, BK, INS and BSA were accurately weighed and dissolved in buffer solution to produce the stock standard solution with the concentrations of 0.5 mg/mL, respectively. The chromatographic separation of analytes was performed on a SinoChrom ODS-BP C18 analytical column (250 mm × 4.6 mm, i.d., 5 μm) (Dalian Elite Analytical Instruments Co. Ltd., Dalian, China). The temperature of the column was


Langmuir 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Page 6 of 23

maintained at 318.15 K. The mobile phase consisted of 70% water and 30% acetonitrile. The flow rate, injection volume, and detection wavelength were set at 1.0 mL/min, 20 μL, and 215 nm, respectively. The wavelength of DA detector ranged from 200 to 400 nm. The regression lines for GSH, BK, INS and BSA were y = 5981.9x − 6.5197 (R2 = 0.9988, n = 5), y = 5095.7x − 50.628 (R2 = 0.9982, n = 5), y = 15875x − 58.186 (R2 = 0.9961, n=5) and y = 4066.8x − 472.36 (R2 = 0.9990, n = 5), respectively, where y is the peak area of biomolecules, and x is biomolecules concentration (mg/mL). Calculation of Adsorption Capacity The adsorption capacities of the N-particles toward biomolecule were evaluated according to the following equation. Adsorption capacity is given as: qt =

(C0 - Ct )V m

(1)

Where qt is the adsorption capacity (mg/g dry N-particles) toward biomolecule at time t. C0 (mg/mL) is the initial concentration of biomolecule. After a period of time t, the raffinate concentration is Ct (mg/mL). V (mL) and m (g) are the adsorbate solution volume and microsphere dry weight, respectively. In addition, the adsorption studies mentioned below were conducted in triplicate, and the deviation error was less than 5%. RESULTS AND DISCUSSION

Figure 2. (a). SEM image of PSE after grinding; (b). SEM images of PSE, (c-h) SEM images of functionalized particles; (c). PSE-CL; (d). PSE-MI; (e). PSE-PPD; (f) PSE-PAA; (g). PSE-DETA;(h) PSE-PDA, respectively.)

Characterization of particles The SEM images of PSE (in Figure 2) shows the morphology and structure of particles. The pictures are the optical images of the corresponding particles. As shown in Figure 2a and Figure S1a, the initial PSE present as uniformed microspheres with diameters of 500-800 μm. Figure 2b shows the enlarged SEM image of


Page 7 of 23 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Langmuir

PSE surface, in which ideal and abundant pore structures were existing. It should be noted that the interior of resin particles also exhibited abundant pore channel. These PSE exhibit relatively homogeneous pores and spherical morphology, while many of the macropore show up in the particles due to the release of water phase. Obviously, surface morphology of the PSE with chemical modification (PSE-MI, PSE-PAA, PSE-PPD and PSE-EDTA) basically the same as the initial PSE. On the contrary, the pore of PSE-PDA had been greatly affected, and the reason had been proved in previous work.24 There are obvious reductions of size and number, which could be proved by comparing internal structure of resins (in Figure S1(b-f)). In addition, the external SEM image of PSE (in Figure 2 (h)) and other SEM image of resin particles modified by chemical method show a clear contrast for pore diameter. These results suggest that the effect of chemical modification on the pore of the resin particles is much lower than that of the physical modification.

Figure 3. (a) Pore size distribution of resins. (b) Nitrogen adsorption and desorption isotherms of resins. (c) Percentage of nitrogen elements and functional degree of resins. (d) Characteristic C1s XPS curves for resins.

The nitrogen adsorption-desorption and BJH pore distribution studies conducted to investigate the surface area and pore structure of resins particles. All resins (in Figure 3 (a) and (b)) show a type Ⅴ isotherm with H1 hysteresis loop with mainly pore diameters in the range of 50-250 nm. In addition, there are also a small number of micropores (< 2 nm) and mesoporous (2-50 nm) in the red box area (Figure 3(a)). However, what calls for special attention is there are hysteresis loop, which is attributed to mesoporous, after modifying becoming larger than PSE. Due to the


Langmuir 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

modification of PSE, the number and volume of the mesoporous of 2~50 nm increased obviously, and the hysteresis loop became larger, after literature research and experimental demonstration, for which we speculate that there are two reasons: (a) channel blocking; (b) capillary condensation.25 The pore size distribution strongly suggests that the mesoporous arising from PSE modification, which makes the inner pore diameter of resin have no change, while the entrance narrows down. As a result, compared to unmodified resin, it is more difficult for nitrogen in the functional PSE pore channel to flow inside (in Figure 4 (a)). On the other hand, for porous polymers, the more mesoporous, the more prone to capillary condensation. It has been mentioned before that the modification of the resin will make some macroporous smaller into the mesoporous, which also causes the hysteresis loop to become larger (in Figure 4 (b)). The BET surface area of functionalized resins were found to be a clear drop, which are well consistent with pore size distribution (in Figure 3 (a)).26

Figure 4. Nitrogen adsorption and desorption profile. (a) Channel blocking: Comparison of nitrogen desorption between PSE and functional PSE; (b) Capillary condensation: Nitrogen accumulation and nitrogen desorption capillary condensation.

To validate successful modification of nitrogenous group, elemental analysis was performed. Based on the N element content before and after PSE modification, the percentage of the N element of all resins change in sequence of PSE (0) < PSE-PPD (0.62%) < PSE-PDA (0.75%) < PSE-DETA (0.78%) < PSE-MI (1.35%) electrostatic interactions > hydrophobic interaction (hydrophobic amino acids >25%) > hydrogen bonds > π–π stacking interaction. Specifically, for the peptide with few hydrophobic amino acids (< 25%) or more hydrogen bond donors, such as arginine, hydrogen bonds interactions was prioritized than hydrophobic interaction. This study aims


Page 18 of 23

Page 19 of 23 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Langmuir

to design specific resins for selected-peptide based on the strategy of interaction mechanism. ASSOCIATED CONTENT Supporting Information The Supporting Information is available free of charge on the ACS Publications website Chloromethylation of PSE, preparation details of PSE-CL, PSE-MI, PSE-PAA, PSE-PPD and PSE-DETA, parameter characterization of super macroporous resins, influence of NaCl concentration for adsorption capacity: adsorption was carried out in PBS pH 7.4, details of hydrogen bonding. ACKNOWLEDGEMENTS The authors acknowledge the financial support of this work by the National Natural Sciences Foundation of China (NSFC No. 21605150 and 21544013), the West Light Foundation of the Chinese Academy of Sciences and Natural Science Foundation of Gansu Province of China (1501RJZA011). AUTHOR INFORMATION Corresponding Authors *E-mail address: [email protected] (Duolong Di). [email protected] (Honglin Zhai). Notes The authors declare no competing financial interest.

REFERENCES (1) Neefjes, J.; Ovaa, H. A peptide's perspective on antigen presentation to the immune system. Nat. Chem. Biol. 2013, 9, 769–775. (2) Nielsen, S. D.; Beverly, R. L.; Qu, Y.; Dallas, D. C. Milk bioactive peptide database: a comprehensive database of milk protein-derived bioactive peptides and novel visualization. Food Chem. 2017, 232, 673–682. (3) Craik, D. J.; Fairlie, D. P.; Spiros, L.; David, P. The future of peptide-based drugs. Chem. Biol. Drug Des. 2013, 81, 136–147. (4) Hilchie, A. L.; Wuerth, K.; Hancock, R. E. Immune modulation by multifaceted cationic host defense (antimicrobial) peptides. Nat. Chem. Biol. 2013, 9, 761–768. (5) Pazos, E.; Vázquez, O.; Mascareñas, J. L.; Vázquez, M. E. Peptide-based fluorescent biosensors. Chem. Soc. Rev. 2009, 38,


Langmuir 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

3348–3359. (6) Croote, D.; Quake, S. R. Food allergen detection by mass spectrometry: the role of systems biology. Npj Syst. Biol. Appl. 2016, 2, 16022–16031. (7) Kim, D. L.; Salazar, O. R.; Nunes, S. P. Membrane manufacture for peptide separation. Green Chem. 2016, 18, 5151–5159. (8) Schäfer, A.; Toerne, C. V.; Becker, S.; Sarioglu, H.; Neschen, S.; Kahle, M. Two-dimensional peptide separation improving sensitivity of selected reaction monitoring-based quantitative proteomics in mouse liver tissue: comparing off-gel electrophoresis and strong cation exchange chromatography. Anal. Chem. 2012, 84, 8853–8862. (9) Motoyama, A.; Xu, T.; Ruse, C. I.; Wohlschlegel, J. A. Anion and cation mixed-bed ion exchange for enhanced multidimensional separations of peptides and phosphopeptides. Anal. Chem. 2007, 79, 3623–3634. (10) Yang, X. Y.; Chen, L. H.; Li, Y.; Rooke, J. C.; Sanchez, C.; Su, B. L. Hierarchically porous materials: synthesis strategies and structure design. Chem. Soc. Rev. 2017, 46, 481–558. (11) Toyoda, M.; Narimatsu, H.; Kameyama, A. Enrichment method of sulfated glycopeptides by a sulfate emerging and ion exchange chromatography. Anal. Chem. 2009, 81, 6140–6147. (12) Michael, S.; Marian, S.; Frantisek, S. “Click Chemistry” in the Preparation of Porous Polymer-Based Particulate Stationary Phases for μ-HPLC Separation of Peptides and Proteins. Anal. Chem. 2006, 78, 4969–4975. (13) Li, B.; Guan, Z.; Wang, W.; Yang, X.; Hu, J.; Tan, B. Highly Dispersed Pd Catalyst Locked in Knitting Aryl Network Polymers for Suzuki–Miyaura Coupling Reactions of Aryl Chlorides in Aqueous Media. Adv. Mater. 2012,24,3390–3395. (14) Seeberger, P. H. Organic synthesis: scavengers in full flow. Nat. Chem. 2009, 1, 258–260. (15) Wang, B.; Prinsen, P.; Wang, H.; Bai, Z.; Wang, H.; Luque, R. Macroporous materials: microfluidic fabrication, functionalization and applications. Chem. Soc. Rev. 2017, 46, 855–914. (16) Kanamori, K.; Hasegawa, J.; Nakanishi, K.; Hanada, T. Facile synthesis of macroporous cross-linked methacrylate gels by atom transfer radical polymerization. Macromolecules 2008, 41, 7186–7193. (17) Goldmann, A. S.; Walther, A.; Nebhani, L.; Joso, R.; Ernst, D.; Loos, K. Surface modification of poly(divinylbenzene) microspheres via thiol−ene chemistry and alkyne−azide click reactions. Macromolecules 2009, 42, 3707–3714. (18) Gokmen, M. T.; Prez, F. E. D. Porous polymer particles—a comprehensive guide to synthesis, characterization, functionalization and applications. Prog. Polym. Sci. 2012, 37, 365–405.


Page 20 of 23

Page 21 of 23 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Langmuir

(19) Wu, D.; Xu, F.; Sun, B.; Fu, R.; He, H.; Matyjaszewski, K. Design and preparation of porous polymers. Chem. Rev. 2012, 112, 3959–4015. (20) Zhao, C. X.; Middelberg, A. P. Microfluidic mass-transfer control for the simple formation of complex multiple emulsions. Angew. Chem. Int. Ed. 2009, 48, 7208–7211. (21) Zhang, D.; Zhou, W.; Li, J. The Construction of an Aqueous Two-Phase System to Solve Weak-Aggregation of Gigaporous Poly(Styrene-Divinyl Benzene) Microspheres. Polymer 2016, 8, 142–146. (22) Qu, J. B.; Zhou, W. Q.; Wei, W.; Su, Z. G.; Ma, G. H. (2008). An effective way to hydrophilize gigaporous polystyrene microspheres as rapid chromatographic separation media for proteins. Langmuir 2008, 24, 13646–13652. (23) Durie, S.; Jerabek, K.; Mason, C.; Sherrington, D. C. One-pot synthesis of branched poly(styrene−divinylbenzene) suspension polymerized resins. Macromolecules 2002, 35(26), 9665–9672. (24) Wang, H.; Qin, Z.; Liu, Y.; Li, X.; Liu, J.; Liu, Y. Design and preparation of porous polymer particles with polydopamine coating and selective enrichment for biomolecules. RSC Adv. 2017, 7, 45311–45319. (25) And, K. M.; Tarui, N. Capillary condensation of nitrogen in ordered mesoporous silica with bicontinuous gyroid structure. J. Phys. Chem. C 2007, 111, 280–285. (26) Wang, X. L.; Mei, J. L.; Zhao, Z.; Zheng, P.; Chen, Z. T.; Gao, D. W.; Fu, J. Y.; Fan, J. Y.; Duan, A. J. Xu, C. M. Self-Assembly of Hierarchically Porous ZSM-5/SBA-16 with Different Morphologies and Its High Isomerization Performance for Hydrodesulfurization of Dibenzothiophene and 4,6-Dimethyldibenzothiophene. ACS Catal. 2018, 8 (3), 1891–1902. (27) Kim, Y.; Moh, L. C. H.; Swager, T. M. Anion exchange membranes: enhancement by addition of unfunctionalized triptycene poly(ether sulfone)s. ACS Appl. Mater. Interfaces 2017, 9, 42409–42414. (28) Morais, A. R. C.; Pinto, J. V.; Nunes, D.; Roseiro, L. B.; Oliveira, M. C.; Fortunato, E. (2015). Imidazole: prospect solvent for lignocellulosic biomass fractionation and delignification. ACS Sustainable Chem. Eng. 2015, 4,1643–1652. (29) Bober, P.; Stejskal, J.; Trchová, M.; Prokeš, J.; Sapurina, I. Oxidation of aniline with silver nitrate accelerated by p-phenylenediamine: a new route to conducting composites. Macromolecules 2010, 43, 10406–10413. (30) Warnke, S.; Seo, J.; Boschmans, J.; Sobott, F.; Scrivens, J. H.; Bleiholder, C. Protomers of benzocaine: solvent and permittivity dependence. J. Am. Chem. Soc. 2015, 137, 4236–4242. (31) Zhang, H.; Dang, Q.; Liu, C.; Cha, D.; Yu, Z.; Zhu, W. Uptake of pb(ii) and cd(ii) on chitosan microsphere surface successively grafted by


Langmuir 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

methyl acrylate and diethylenetriamine. ACS Appl. Mater. Interfaces 2017, 9, 11144–11155. (32) Miyamoto, M.; Harada, Y.; Tobisu, M.; Chatani, N. Rh(i)-catalyzed reaction of 2-(chloromethyl)phenylboronic acids and alkynes leading to indenes. Org. Lett. 2008, 39, 2975–2978. (33) Zheng, B.; Sugiyama, M.; Eastgate, M. D.; Fritz, A.; Murugesan, S.; Conlon, D. A. (2012). Development of a process for the preparation of chloromethyl chlorosulfate. Org. Process Res. Dev. 2012,16, 1827–1831. (34) Micksch, T.; Liebelt, N.; Scharnweber, D. Schwenzer, B. Investigation of the peptide adsorption on ZrO2, TiZr, and TiO2 surfaces as a method for surface modification. ACS Appl. Mater. Interfaces 2014, 6, 7408–7416. (35) Lou, S.; Chen, Z.; Liu, Y.; Ye, H.; Di, D. New way to analyze the adsorption behavior of flavonoids on macroporous adsorption resins functionalized with chloromethyl and amino groups. Langmuir 2011, 27, 9314–9326. (36) Liu, Y.; Di, D.; Bai, Q.; Li, J.; Chen, Z.; Lou, S. Preparative separation and purification of rebaudioside a from steviol glycosides using mixed-mode macroporous adsorption resins. J. Agric. Food. Chem. 2011, 59, 9629–9636. (37) Khullar, P.; Singh, V.; Mahal, A.; Dave, P. N.; Thakur, S.; Kaur, G. Bovine serum albumin bioconjugated gold nanoparticles: synthesis, hemolysis, and cytotoxicity toward cancer cell lines. J. Phys. Chem. C 2012, 116, 8834–8843. (38) Nadendla, K.; Friedman, S. H. Light control of protein solubility through isoelectric point modulation. J. Am. Chem. Soc. 2017, 139, 17861–17869. (39) Schmidt, M. M.; Koehler, Y.; Derr, L.; Treccani, L.; Rezwan, K.; Dringen, R. Interaction of the physiological tripeptide glutathione with colloidal alumina particles. J. Phys. Chem. C 2013, 116, 23136–23142. (40) Huo, S. H,; Yan, X. P. Metal–organic framework MIL-100(Fe) for the adsorption of malachite green from aqueous solution. J. Mater. Chem. 2012, 22(15):7449–7455. (41) Krauland, E. M.; Peelle, B. R.; Wittrup, K. D.; Belcher, A. M. Peptide tags for enhanced cellular and protein adhesion to single-crystalline sapphire. Biotechnol. Bioeng. 2007, 97, 1009–1020.


Page 22 of 23

Page 23 of 23 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Langmuir

83x46mm (300 x 300 DPI)


Investigation on Adsorption Mechanism of Peptides with Surface

Recommend Documents