Langmuir-Blodgett (LB)-based nanobiocrystallography at the frontiers of cancer proteomics

Abstract

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.

Keywords: Cancer; KINARI mutagen web-server; LB-based nanocrystallography; casein kinase II (CK2); in silico systematic mutagenesis; proteomics; ribonuclease A (RNase A).