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The binding of flavopiridol to blood serum albumin
Author(s) -
Myatt Daniel,
Johnson Louise,
Baumli Sonja,
Siligardi Giuliano
Publication year - 2010
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.20925
Subject(s) - chemistry , bovine serum albumin , circular dichroism , albumin , human serum albumin , serum albumin , plasma protein binding , biochemistry
Flavopiridol is a potent cyclin‐dependant kinase (CDK) inhibitor and is in clinical trials for anticancer treatment. A limiting factor in its drug development has been the high dosage required in human clinical trials. The high dosage is suggested to be necessary because of significant flavopiridol binding to human blood serum. Albumin is the major protein component of blood serum and has been suggested as a likely high affinity binding target. We characterized the binding of human serum albumin to flavopiridol using circular dichroism (hereafter CD). Flavopiridol bound to human serum albumin has a diagnostic CD binding peak at 284 nm. The diagnostic CD binding peak was unobservable for flavopiridol with bovine serum albumin, using the same experimental conditions. However, under higher albumin concentrations a small CD signal is observed confirming, flavopiridol binds to bovine serum albumin as well. Chirality 22:E40–E43, 2010. © 2010 Wiley‐Liss, Inc.