Linnan Xu

Recent advances in applications of nanomaterials for sample preparation

Sample preparation is a key step for qualitative and quantitative analysis of trace analytes in complicated matrix. Along with the rapid development of nanotechnology in material science, numerous nanomaterials have been developed with particularly useful applications in analytical chemistry. Benefitting from their high specific areas, increased surface activities, and unprecedented physical/chemical properties, the potentials of nanomaterials for rapid and efficient sample preparation have been exploited extensively. In this review, recent progress of novel nanomaterials applied in sample preparation has been summarized and discussed. Both nanoparticles and nanoporous materials are evaluated for their unusual performance in sample preparation. Various compositions and functionalizations extended the applications of nanomaterials in sample preparations, and distinct size and shape selectivity was generated from the diversified pore structures of nanoporous materials. Such great variety make nanomaterials a kind of versatile tools in sample preparation for almost all categories of analytes.

SnO2–ZnSn(OH)6: a novel binary affinity probe for global phosphopeptide detection

ZnSn(OH)(6) and binary-component SnO(2)-ZnSn(OH)(6) were introduced as affinity probes for phosphopeptide enrichment for the first time. Two strategies, either ZnSn(OH)(6) and SnO(2) serial enrichment or binary-component SnO(2)-ZnSn(OH)(6) enrichment in a single run, were proposed to enhance multi-phosphopeptide enrichment and to significantly improve global phosphopeptide detection.

Template-free synthesis of uniform mesoporous SnO2 nanospheres for efficient phosphopeptide enrichment

A one-step and template-free method to prepare uniform SnO2 nanospheres with a mesoporous structure was developed for the applications in phosphopeptide enrichment. The as-synthesized mesoporous SnO2 nanospheres have a large surface area and highly active surfaces for the effective binding of phosphopeptides. Compared with the non-porous SnO2 and commercial TiO2, mesoporous SnO2 nanospheres represent superior performance in the specific trapping of phosphopeptides from both standard protein and complex nonfat milk digests for mass spectrometry-based phosphoproteomic analysis. The feasible synthetic approach and the excellent enrichment performance make the mesoporous SnO2 nanospheres promising in further phosphoproteomic research.

Novel nanomaterials used for sample preparation for protein analysis

AbstractSample preparation is of vital importance for proteomic analysis because of the high complexity of biological samples. The rapid development of novel nanomaterials with various compositions, morphologies, and proper surface modifications provides a category of powerful tools for the sample preparation for protein analysis. In this paper, we have summarized recent progresses for the applications of novel nanomaterials in sample preparation for the analysis of proteomes, especially for phosphoproteomes, glycoproteomes, and peptidoms. Several kinds of novel nanomaterials were also discussed for their use in other kinds of proteomics analysis. Graphical abstractIllustration of sample preparation methods by nanomaterials for protein analysis

Cysteine-Functionalized Metal–Organic Framework: Facile Synthesis and High Efficient Enrichment of N-Linked Glycopeptides in Cell Lysate

Cysteine-functionalized metal-organic framework (MOF) was synthesized via a common and facile two-step method of in situ loading of Au nanoparticles on amino-derived MOF followed by l-cysteine (Cys) immobilization. Owing to the large specific surface area and ultrahigh hydrophilicity of this nanocomposite, excellent performance was observed in the enrichment of N-linked glycopeptides in both model glycoprotein and HeLa cell lysate. By using this nanocomposite, 16 and 31 glycopeptides were efficiently extracted from digest of horseradish peroxidase (HRP) and human serum immunoglobulin G (IgG), respectively. The short incubation time (5 min), large binding capacity (150 mg/g, IgG digest to material), good selectivity (1:50, molar ratio of IgG and bovine serum albumin (BSA) digest), high recovery (over 80%), and low detection limit (1 fmol) ensure the effectiveness and robustness of MIL-101(NH2)@Au-Cys in complex HeLa cell lysate. As a result, 1123 N-glycosylation sites corresponding to 1069 N-glycopeptides and 614 N-glycoproteins were identified from the lysate. Compared with those of previously reported hydrophilic methods, to our knowledge, it was the best result. This work paves a new way for fast functionalization of MOF and also provides a novel idea for material design in sample preparation, especially in glycoproteome and related analysis.

Online coupling techniques in ambient mass spectrometry.

Since ambient mass spectrometry (AMS) has been proven to have low matrix effects and high salt tolerance, great efforts have been made for online coupling of several analytical techniques with AMS. These analytical techniques include gas chromatography (GC), liquid chromatography (LC), capillary electrophoresis (CE), surface plasmon resonance (SPR), and electrochemistry flow cells. Various ambient ionization sources, represented by desorption electrospray ionization (DESI) and direct analysis in real time (DART), have been utilized as interfaces for the online coupling techniques. Herein, we summarized the advances in these online coupling methods. Close attention has been paid to different interface setups for coupling, as well as limits of detection, tolerance to different matrices, and applications of these new coupling techniques.

Binding constant determination of uranyl-citrate complex by ACE using a multi-injection method.

The binding constant determination of uranyl with small‐molecule ligands such as citric acid could provide fundamental knowledge for a better understanding of the study of uranyl complexation, which is of considerable importance for multiple purposes. In this work, the binding constant of uranyl–citrate complex was determined by ACE. Besides the common single‐injection method, a multi‐injection method to measure the electrophoretic mobility was also applied. The BGEs used contained HClO4 and NaClO4, with a pH of 1.98 ± 0.02 and ionic strength of 0.050 mol/L, then citric acid was added to reach different concentrations. The electrophoretic mobilities of the uranyl–citrate complex measured by both of the two methods were consistent, and then the binding constant was calculated by nonlinear fitting assuming that the reaction had a 1:1 stoichiometry and the complex was [(UO2)(Cit)]−. The binding constant obtained by the multi‐injection method was log K = 9.68 ± 0.07, and that obtained by the single‐injection method was log K = 9.73 ± 0.02. The results provided additional knowledge of the uranyl–citrate system, and they demonstrated that compared with other methods, ACE using the multi‐injection method could be an efficient, fast, and simple way to determine electrophoretic mobilities and to calculate binding constants.