Summarizing Solvation Effects on Antibody Structure and Function

Ramachandran Murali, Somdutta Saha, Anastas Pashov, Thomas Kieber-Emmons

Department of Biological Sciences, Research Division of Immunology, Cedars-Sinai Medical Center, Los Angeles, CA, USA. Winthrop P. Rockefeller Cancer Institute, University of Arkansas for Medical Sciences, Little Rock, AR, USA. Stephan Angelov Institute of Microbiology, Bulgarian Academy of Sciences, Sofia, Bulgaria

Protein interactions at the atomic-scale are influenced by the solvent microenvironment, playing a role in molecular recognition by modulating a direct relationship between biological (macroscopic solvent) function and effects on protein binding mechanisms. The antibody molecule is a prototypical protein for understanding molecular recognition, binding and evolution in function. The first order biological function of antibodies is to bind to antigens. While a wealth of knowledge accumulated in understanding solvent mediated antibody structure stability, the role of solvent and its relationship to evolution (i.e., affinity maturation or antigen mimicry) and antibody polyspecificity is poorly understood. Recently, we examined how the solvent microenvironment affects antibody flexibility and the molecular interactions that define the recognition of the neolactoseries antigen Lewis Y (LeY), designated tumor-antigen associated with several solid cancers. In particular, we were interested in how antibodies that are close in sequence to antibody germline genes can distinguish glycans considering the effect of solvent microenvironment on the recognition process. Here, we place our results in context of a broader viewpoint of antibody interactions and significance in developing antibody-based therapeutics. Journal of Nature and Science (JNSCI), 3(7):e402, 2017

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