Abstract
The nature of the binding mechanism between the B12H12SH-2 anion (BSH) and serum albumin has long been a question.1–3 Early experimente(1,2) suggested that BSH may be bound covalently to the albumin molecule via a disulfide bond, since the interaction of BSH to albumin was somewhat stronger than that of B12H -212 . One problem with many of the previous experiments concerned with the binding of BSH to albumin was that a method was not readily available with which to directly determine the nature of the interaction without significant disruption of the system. Recently, nuclear magnetic resonance (NMR) spectroscopy has been used to determine that covalent bonding via the formation of disulfide bonding is not significantly involved in the binding mechanism.(4)
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Bauer, W.F., Bradshaw, K.M., Richards, T.L. (1992). Interaction between Boron Containing Compounds and Serum Albumin Observed by Nuclear Magnetic Resonance. In: Allen, B.J., Moore, D.E., Harrington, B.V. (eds) Progress in Neutron Capture Therapy for Cancer. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3384-9_74
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DOI: https://doi.org/10.1007/978-1-4615-3384-9_74
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