Preparation and application of peptide molecular imprinted material based on mesoporous metal-organic framework
Fig.2 XRD patterns of (a) simulated UiO-66-NH2, (b)microporous UiO-66-NH2, (c)mesoporous UiO-66-NH2 and (d) mesoporous MIP@UiO-66-NH2. Fig.3 SEM images of (a)microporous UiO-66-NH2, (b) mesoporous UiO-66-NH2 and (c) mesoporous MIP@UiO-66-NH2; TEM images of (d) microporous UiO-66-NH2 (e) mesoporous UiO-66-NH2 and (f) mesoporous MIP@UiO-66-NH2 Fig.4 N2 sorption isotherms of (a) UiO-66-NH2 (b) UiO-66-NH2 after decarboxylation (c) mesoporous MIP@UiO-66-NH2 and pore sizes distribution of (d) UiO-66-NH2 (e) UiO-66-NH2 after decarboxylation (f) mesoporous MIP@UiO-66-NH2 Fig.5 The effects of pore size and dosage of MOFs on the adsorption capacity of MIP@UiO-66-NH2.Polymerization conditions: mGSH=100 mg, mAM=0.72 g, mNVP=0.56 g, mNMBA=10 mg, and mDMDAAC=0.14 g; adsorption conditions:cGSH,0=0.1 g·L-1, V=1 mL, mMIP=1 mg, t=4 h, pH=7.00, T=4 ℃; eluent : CH3OH/HAc (9/1, v/v) Fig.6 The effect of the ratio of cross-linking agents and functional monomers on the adsorption capacity of MIP@UiO-66-NH2.Polymerization conditions: mGSH=100 mg, mmesoporous UiO-66-NH2=100 mg, other conditions see Fig.5 Fig.7 The effect of eluent on the adsorption capacity of MIP@UiO-66-NH2. Polymerization conditions: mGSH=100 mg, mmesoporous UiO-66-NH2=100 mg, mAM=0.72 g, mNVP=0.56 g, mNMBA=2 mg, mDMDAAC=0.028 g; other conditions see Fig.5 Fig.8 (a)Adsorption isotherm, (b) the Langmuir model, (c) the Freundlich model of MIP@UiO-66-NH2.Adsorption conditions see Fig.5; polymerization conditions see fig.7, eluent: 1% SDS/10% HAc (w/v) Fig.9 Kinetic adsorption curves and kinetic model fitting curves of (a) Pseudo-first order model and (b) Pseudo-second order model of MIP@UiO-66-NH2 at different temperatures. Adsorption conditions: t=1, 2, 5, 10, 20, 30, 40, 50, 60, 120 min, T=4℃, 25℃, 37℃, other conditions see Fig.5; polymerization conditions see Fig.7; eluent:1% SDS/10% HAc (w/v) Fig.10 The MALDI-TOF mass spectra:(a) the remaining solution after adsorption (the loading condition: 0.10 g·L-1of GSH and 0.10 g·L-1 BSA tryptic digest) (b) the obtained eluent, (c) the remaining solution after adsorption (the loading condition:0.10 g·L-1 of GSH and 1.0 g·L-1 BSA tryptic digest),(d) the obtained eluent (★indicates GSH) Fig.11 The MALDI-TOF mass spectra:(a) the remaining solution after adsorption (the loading condition: 500 μL 0.10 g·L-1of GSH and 500 μL skim milk tryptic digest) (b) the obtained eluent, (c) the remaining solution after adsorption (the loading condition: 500 μL 0.10 g·L-1of GSH and 500 μL egg white tryptic digest),(d) the obtained eluent (★indicates GSH)
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Materials and Reagents N,N-dimethylformamide (DMF), Zirconium oxychloride (ZrOCl2), N,N′-methylene-bis-acrylamide (NMBA), 5,5'-dithio bis-(2-nitrobenzoic acid) (DTNB) and phosphoric acid (H3PO4) were purchased from Aladdin Company (Shanghai, China). 1,4-dicarboxybenzene (H2BDC), 2-aminoterephthalic acid (H2BDC-NH2) and L-ascorbic acid (L-Vc) were purchased from Dibo Biological Technology Company (Shanghai, China). Ethanol (C2H5OH), acetic acid (HAc) and dibasic sodium phosphate (Na2HPO4) were purchased from Lingfeng Company (Shanghai, China). Silver nitrate (AgNO3) and potassium persulfate (K2S2O8) were purchased from Titan Technology Company (Shanghai, China). Acrylamide (AM), glutathione and N-vinylpyrrolidone (NVP) were purchased from Macklin (Shanghai, China). Dimethyl diallyl ammonium chloride (DMDAAC) was purchased from Tixiai Chemical Industry Development Company (Shanghai, China). Hydrogen peroxide (H2O2, 30%) was purchased from Sinopharm Chemical Reagent Company (Shanghai, China). Sodium lauryl sulfate (SDS) was purchased from Nantong Feiyu Biological Technology Co., Ltd. (Shanghai, China). Urea, ammonium bicarbonate(NH4HCO3), trypsin (TPCK treated Trypson，10,000 U/mg ), bovine albumin (BSA), dithiothreitol (DTT) and iodoacetamide (IAA) were purchased from Sigma-Aldrich Company(America). Ultrapure water, purified with a Milli-Q system (Millipore, Milford, MA, USA), was used to prepare all solutions. Other chemical reagents were of analytical grade. Apparatus for characterization The morphologies of the MOFs and MIPs were observed by transmission electron microscope (JEOL2100 HR, Tokyo, Japan) and scan electron microscope (Hitachi S-3400N, Tokyo, Japan). Brunauer–Emmett–Teller surface area was obtained from nitrogen adsorption/desorption experiments (QUADRASORB SI, USA). The structure of the powder samples was characterized by Rotating Anode X-ray Powder Diffractometer (18KW/D/max2550VB/PC, Japan). Element analysis was carried out with an elemental analyzer (C、H、N、S ⅱ/VARIO ELⅢ , ELEMENTAR，Germany). The GSH and other analogues were determined by MALDI-TOF system (AB Sciex 4800 plus, AB Sciex, USA). Mass Spectrometry All MALDI-TOF mass data were obtained from AB Sciex 4800 Plus MALDI TOF/TOF Analyzer (AB Sciex, CA) at 355 nm and 200 Hz in reflector positive mode. Matrix DHB was dissolved in 70 % ACN-H2O containing 1 % H3PO4 for the analysis of peptides (25 mg·mL-1). 0.5 μL eluate of peptides or proteins was dropped onto the MALDI plate and dried at room temperature, and then 0.5 μL DHB matrix solution was added and dried for MS analysis.