Background/aim: Langmuir-Blodgett (LB) films used as templates for crystallization lead to marked changes in protein stability and water dehydration, despite slight changes in protein atomic structure. Herein, we discuss the importance of LB-based nanocrystallography at the frontiers of cancer proteomics focusing on two model proteins with important biological roles in cancer, namely CK2alpha and RNase A.
Materials And Methods: Computational mutagenesis using the KINARI Mutagen webserver exhibits different behaviors in terms of stability and robustness, as well as in terms of water dynamics.
Conclusion: Introduction of LB film leads to the appearance of water molecules close to the protein surface with larger volume, causing changes in crystal stability against radiation and appearing replicated in mutant proteins. Implications for drug design, drug delivery and cancer-causing protein variants are herein presented, along with a review of the most recent findings in LB-based nanobiocrystallography.
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Langmuir-Blodgett (LB)-based nanobiocrystallography at the frontiers of cancer proteomics.
Anticancer Res
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Nanoworld Institute, Fondazione EL.B.A. Nicolini (FEN), Pradalunga, Bergamo, Italy Laboratories of Biophysics and Nanobiotechnology (LBN), Department of Medical Science, University of Genova, Genova, Italy European Synchrotron Radiation Facility (ESRF), Grenoble, France
Background/aim: Langmuir-Blodgett (LB) films used as templates for crystallization lead to marked changes in protein stability and water dehydration, despite slight changes in protein atomic structure. Herein, we discuss the importance of LB-based nanocrystallography at the frontiers of cancer proteomics focusing on two model proteins with important biological roles in cancer, namely CK2alpha and RNase A.
Materials And Methods: Computational mutagenesis using the KINARI Mutagen webserver exhibits different behaviors in terms of stability and robustness, as well as in terms of water dynamics.
Advances in nanocrystallography as a proteomic tool.
Adv Protein Chem Struct Biol
April 2018
Nanobiotechnology and Biophysics Laboratories (NBL), Department of Experimental Medicine (DIMES), University of Genoa, Genoa, Italy; Nanoworld Institute Fondazione ELBA Nicolini (FEN), Pradalunga, Bergamo, Italy; Biodesign Institute, Arizona State University, Tempe, Arizona, USA. Electronic address:
In order to overcome the difficulties and hurdles too much often encountered in crystallizing a protein with the conventional techniques, our group has introduced the innovative Langmuir-Blodgett (LB)-based crystallization, as a major advance in the field of both structural and functional proteomics, thus pioneering the emerging field of the so-called nanocrystallography or nanobiocrystallography. This approach uniquely combines protein crystallography and nanotechnologies within an integrated, coherent framework that allows one to obtain highly stable protein crystals and to fully characterize them at a nano- and subnanoscale. A variety of experimental techniques and theoretical/semi-theoretical approaches, ranging from atomic force microscopy, circular dichroism, Raman spectroscopy and other spectroscopic methods, microbeam grazing-incidence small-angle X-ray scattering to in silico simulations, bioinformatics, and molecular dynamics, has been exploited in order to study the LB-films and to investigate the kinetics and the main features of LB-grown crystals.
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