title: Langmuir-Blodgett (LB)-based nanobiocrystallography at the frontiers of cancer proteomics.
abstract: OBJECTIVE
  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.
  
  
  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.
  
  
  CONCLUSIONS
  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.
authors: 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.
authors: Eugenia
authors: E
authors: Pechkova
authors: 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.
authors: Nicola Luigi
authors: NL
authors: Bragazzi
authors: 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.
authors: Stefano
authors: S
authors: Fiordoro
authors: 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 president@fondazioneelba-nicolini.org.
authors: Claudio
authors: C
authors: Nicolini
mesh_terms: D001709:Biotechnology / Q000379:methods*; D003461:Crystallography / Q000379:methods*; D008958:Models, Molecular; D009363:Neoplasm Proteins / Q000737:chemistry*; D040901:Proteomics
chemical_list: D009363:Neoplasm Proteins
keywords: Cancer; KINARI mutagen web-server; LB-based nanocrystallography; casein kinase II (CK2); in silico systematic mutagenesis; proteomics; ribonuclease A (RNase A)