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Author(s): Pathan Najiya Shahnoor*1, Sayyad Simran Shabbir2, Shaikh Sadiya Mehmood3, Ansari Shaheenanjum Babuddin4, Dr. Aejaz Ahmed5, Dr. G. J. Khan.6

Email(s): 1najiyasp@gmail.com

Address:

    J.I.I.U' S Ali Allana College of Pharmacy Akkalkuwa, Dist. Nandurbar (425415), Maharashtra, India

Published In:   Volume - 2,      Issue - 5,     Year - 2023

DOI: Not Available

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ABSTRACT:
With the introduction of soft ionization techniques such as Matrix Assisted Laser Desorption Ionization (MALDI), and Electrospray Ionization (ESI), proteins have become accessible for mass spectrometric analyses. Since then, mass spectrometry has emerged as the preferred technique for identifying proteins and peptides at a low cost, with high reliability and sensitivity. With a growing number of complete genome sequences available for a wide range of organisms and multiple protein databases built from them, mass spectrometry can now identify proteins with high throughput. This Review discusses the suitability of strategies for automated data analysis and provides a brief overview of methods for identifying posttranslational modifications, highlighting the various mass spectrometric techniques currently used in proteome research. In the biopharmaceutical sector, mass spectrometry (MS) is the main analytical method used to identify proteins. The gold standard method for analysing intact proteins is to combine liquid chromatography with electrospray ionisation (ESI). Nevertheless, speed constraints make it impossible to analyse big sample sizes (>1000) in a single day. On a high throughput IR-MALDESI-MS system, proteins as small as 150 kDa can be detected, and we have assessed the impact of the matrix on the signal. Up to 22 protein samples can be analysed by the system in a single second. Applications include compound modifications to a probe protein, compound binding kinetics, and protein autophosphorylation. A cysteine modification site was found using top-down protein sequencing.

Cite this article:
Pathan Najiya Shahnoor, Sayyad Simran Shabbir, Shaikh Sadiya Mehmood, Ansari Shaheenanjum Babuddin, Dr. Aejaz Ahmed, Dr. G. J. Khan. High Throughput Protein Analysis Enabled by IR, MALDI, ESI, MS. IJRPAS, Sep-Oct 2023; 2(5): 185-203.


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3.      https://en.wikipedia.org/wiki/Matrix-assisted_laser_desorption/ionization

4.      20 Douglas A. Skoog, Stanley R. Crouch, and F. James Holler, "Principles of Instrumental Analysis," Seventh Edition,2016-page no.509,510.

5.      Judith Webster and David Oxley” Protein Identification by MALDI-TOF Mass Spectrometry” DOI 10.1007/978-1-61779-349-3_15, © Springer Science Business Media, LLC 2012

6.      Šebela, M. Biomolecular Profiling by MALDI-TOF Mass Spectrometry in Food and Beverage Analyses. Int. J. Mol. Sci. 2022, 23, 13631. https://doi.org/10.3390/ ijms232113631 Published: 7 November 2022

7.      https://www.mdpi.com/journal/ijms.Int.J.Mol.Sci.2022,23, 13631.https://doi.org/10.3390/ijms232113631

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9.      Donna M. Wolk, Andrew E. Clark, https://doi.org/10.1016/j.cll.2018.05.008 0272-2712/18/ª 2018

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11.  Sven Schuchardt1 and Albert Sickmann” Protein identification using mass spectrometry: A method overview” DOI: 10.1007/978-3-7643-7439-6_7 · Source: PubMed February 2007.

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13.  Fan Pu, Scott A. Ugrin, Andrew J. Radosevich, David Chang-Yen, James W. Sawicki, Nari N. Talaty, Nathaniel L. Elsen  and Jon D. Williams” High Throughput Intact Protein Analysis Using Infrared Matrix-Assisted Laser Desorption Electrospray Ionization Mass Spectrometry” doi: https://doi.org/10.1101/2021.11.08.467755; December 18, 2021

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