TY - JOUR
T1 - Chemical crosslinking
T2 - Role in protein and peptide science
AU - Arora, Bharti
AU - Tandon, Rashmi
AU - Attri, Pankaj
AU - Bhatia, Rohit
N1 - Funding Information:
RB acknowledges Director, Institute Of Home Economics for her constant encouragement and support. PA gratefully acknowledges the grant provided by the SRC program of the National Research Foundation of Korea (NRF), funded by the Korean Government Ministry of Education, Science and Technology (MEST) (No. 20100029418) and in part by Kwangwoon University 2015. PA is thankful to FY 2015 Japan Society for the Promotion of Science 501100001691 (JSPS) invitation fellowship.
Publisher Copyright:
© 2017 Bentham Science Publishers.
PY - 2017
Y1 - 2017
N2 - Background: Chemical crosslinking refers to intermolecular or intramolecular joining of two or more molecules by a covalent bond. The reagents that are used for the purpose are referred to as ‘crosslinking reagents’ or ‘crosslinkers’. Based on factors like reactivity and spacer length these are classified into different types, each having its own specific function and application. In recent times, chemical crosslinking has emerged as an efficient tool for the study of biomolecules like proteins. It finds its application in various studies including the attachment of proteins to a solid support for the study of membrane receptors, protein-protein complexes, protein-DNA complexes, and others. When coupled with techniques like mass spectroscopy, it has been used not only for the determination of three dimensional structures of proteins but also for the study of protein-protein interactions and determination of interesting sites. This combination of mass spectrometry techniques and bioinformatics, added yet another dimension to our present day understanding of protein chemistry. Thus, chemical crosslinking has multitude uses that it can be put to. Methods: We undertook a systematic search of bibliographic databases and search engine such as Google Scholar, Scifinder, Scopus, Mendeley etc for review of research literature. We excluded research paper which only reported synthesis of crosslinker molecules and did not involve any mass spectrometry studies. Results: Sixty-four papers were included in the review. The majority of references were taken from last ten years as there has been an immense progress in this area in the recent years. Eleven classical papers in this field were included which talk about basic of this methodology. Thirty-two papers discussed about various types of organic groups used for designing chemical cross-linkers and various methodologies which were used to enhance the crosslinking efficiency. These papers also highlight various strategies used to enhance detection of cross-linked proteins and various computer software used to detect cross-linking sites from mass data. Twenty-one papers showed the proof concept application of this methodology to detect protein crosslinking in-vivo and in-vitro. Conclusion: The findings of this review confirm the importance chemical crosslinking combined with mass spectroscopy as a low cost alternative to understand protein-protein interaction. The information generated by this methodology can help in better understating of various diseases and for the development of better drugs for them.
AB - Background: Chemical crosslinking refers to intermolecular or intramolecular joining of two or more molecules by a covalent bond. The reagents that are used for the purpose are referred to as ‘crosslinking reagents’ or ‘crosslinkers’. Based on factors like reactivity and spacer length these are classified into different types, each having its own specific function and application. In recent times, chemical crosslinking has emerged as an efficient tool for the study of biomolecules like proteins. It finds its application in various studies including the attachment of proteins to a solid support for the study of membrane receptors, protein-protein complexes, protein-DNA complexes, and others. When coupled with techniques like mass spectroscopy, it has been used not only for the determination of three dimensional structures of proteins but also for the study of protein-protein interactions and determination of interesting sites. This combination of mass spectrometry techniques and bioinformatics, added yet another dimension to our present day understanding of protein chemistry. Thus, chemical crosslinking has multitude uses that it can be put to. Methods: We undertook a systematic search of bibliographic databases and search engine such as Google Scholar, Scifinder, Scopus, Mendeley etc for review of research literature. We excluded research paper which only reported synthesis of crosslinker molecules and did not involve any mass spectrometry studies. Results: Sixty-four papers were included in the review. The majority of references were taken from last ten years as there has been an immense progress in this area in the recent years. Eleven classical papers in this field were included which talk about basic of this methodology. Thirty-two papers discussed about various types of organic groups used for designing chemical cross-linkers and various methodologies which were used to enhance the crosslinking efficiency. These papers also highlight various strategies used to enhance detection of cross-linked proteins and various computer software used to detect cross-linking sites from mass data. Twenty-one papers showed the proof concept application of this methodology to detect protein crosslinking in-vivo and in-vitro. Conclusion: The findings of this review confirm the importance chemical crosslinking combined with mass spectroscopy as a low cost alternative to understand protein-protein interaction. The information generated by this methodology can help in better understating of various diseases and for the development of better drugs for them.
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U2 - 10.2174/1389203717666160724202806
DO - 10.2174/1389203717666160724202806
M3 - Review article
C2 - 27455969
AN - SCOPUS:85011559267
VL - 18
JO - Current Protein and Peptide Science
JF - Current Protein and Peptide Science
SN - 1389-2037
IS - 2
ER -