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      Hexagonal Mesoporous Silica as a Rapid, Efficient and Versatile Tool for MALDI-TOF MS Sample Preparation in Clinical Peptidomics Analysis: A Pilot Study

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          Abstract

          Improvement in high-throughput MALDI-TOF MS analysis requires practical and efficient sample preparation protocols for high acquisition rates. The use of hexagonal mesoporous silica (HMS) sorbents in combination with MALDI-TOF MS was explored as a versatile tool for peptidomic profiling of clinical specimens difficult to process, but considered important sources of disease biomarkers: synovial fluid and sputum. A rapid and efficient procedure, based on dispersive solid-phase extraction of peptides using commercially available wormhole mesostructured HMS, was tested for: a) pre-concentration of standard peptides in serially diluted solution up to the sub-nanomolar range; b) peptidome profiling of sputum and synovial fluid. The use of HMS, as dispersed sponges, significantly amplified the peptidic repertoire of sputum and synovial fluid by excluding from the adsorptive process large size proteins, which mask and/or suppress peptidome signals. The protocol proposed, as dispersive solid phase extraction, ensures good analytical performances. Moreover, it is economical and rapid, as it avoids the use of less reproducible and prolonged sample preparation procedures, such as the use of ultrafiltration filter devices. These findings may contribute to defining a high-throughput screening MS-based platform for monitoring key peptidic features of difficult to analyse bodily fluids in a clinical setting.

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          Most cited references35

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          A neutral templating route to mesoporous molecular sieves.

          A neutral templating route for preparing mesoporous molecular sieves is demonstrated based on hydrogen-bonding interactions and self-assembly between neutral primary amine micelles (S degrees ) and neutral inorganic precursors (l degrees ). The S degrees l degrees templating pathway produces ordered mesoporous materials with thicker framework walls, smaller x-ray scattering domain sizes, and substantially improved textural mesoporosities in comparison with M41S materials templated by quaternary ammonium cations of equivalent chain length. This synthetic strategy also allows for the facile, environmentally benign recovery of the cost-intensive template by simple solvent extraction methods. The S degrees 1 degrees templating route provides for the synthesis of other oxide mesostructures (such as aluminas) that may be less readily accessible by electrostatic templating pathways.
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            Human body fluid proteome analysis.

            The focus of this article is to review the recent advances in proteome analysis of human body fluids, including plasma/serum, urine, cerebrospinal fluid, saliva, bronchoalveolar lavage fluid, synovial fluid, nipple aspirate fluid, tear fluid, and amniotic fluid, as well as its applications to human disease biomarker discovery. We aim to summarize the proteomics technologies currently used for global identification and quantification of body fluid proteins, and elaborate the putative biomarkers discovered for a variety of human diseases through human body fluid proteome (HBFP) analysis. Some critical concerns and perspectives in this emerging field are also discussed. With the advances made in proteomics technologies, the impact of HBFP analysis in the search for clinically relevant disease biomarkers would be realized in the future.
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              Mesoporous Silica Molecular Sieves Prepared by Ionic and Neutral Surfactant Templating:  A Comparison of Physical Properties

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                Author and article information

                Contributors
                Role: Academic Editor
                Role: Academic Editor
                Journal
                Molecules
                Molecules
                molecules
                Molecules
                MDPI
                1420-3049
                22 June 2019
                June 2019
                : 24
                : 12
                : 2311
                Affiliations
                [1 ]Department of Health Sciences, University “Magna Græcia”, 88100 Catanzaro, Italy; preiano@ 123456unicz.it (M.P.); giusimaggisano@ 123456unicz.it (G.M.); savino@ 123456unicz.it (R.S.)
                [2 ]Department of Medical and Surgical Sciences, University “Magna Græcia”, 88100 Catanzaro, Italy; pelaia.corrado@ 123456gmail.com
                Author notes
                [* ]Correspondence: terracciano@ 123456unicz.it ; Tel.: +39-0961-3694085; Fax: +39-0961-3694090
                Article
                molecules-24-02311
                10.3390/molecules24122311
                6631377
                31234484
                d8e5e2d5-8b88-4963-933c-35a86add3cd6
                © 2019 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 29 April 2019
                : 20 June 2019
                Categories
                Article

                maldi-tof,peptidomics,profiling,fingerprinting,biomarkers,sample preparation,analytical chemistry

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