title: Commentary on "spectral characterization of the binding and conformational changes of serum albumins upon interaction with an anticancer drug, anastrozole".
abstract: The manuscript by R. Punith and J. Seetharamappa (http://dx.doi.org/10.1016/j.saa.201202.038) presents the interaction between serum albumin from human (HAS) and from bovine (BSA) with a drug called Anastrozole (AZ). The drug is on the market for treating patients with breast cancer after surgery and for metastasis in women. The study utilizes various spectroscopic techniques such as; fluorescence, synchronous fluorescence, 3D fluorescence measurements, FTIR, CD and UV. Although there are some relatively minor comments on the paper, the main point that needs to be reviewed by the authors is the result of FTIR measurements. Based on the data provided in the text (there is no figure), the protein sample is not in its native state, which makes the data inconvenient to be used in drawing conclusions. Authors are kindly requested to take another look at the FTIR experiments.
authors.affiliation: Atilim University, Physics Unit, Biophysics Laboratory, Ankara 06836, Turkey.
authors.forename: Filiz
authors.initials: F
authors.lastname: Korkmaz
mesh_terms: D000818:Animals; D018931:Antineoplastic Agents, Hormonal / Q000378:metabolism*; D006801:Humans; D009570:Nitriles / Q000378:metabolism*; D012709:Serum Albumin / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D014230:Triazoles / Q000378:metabolism*
chemical_list: D018931:Antineoplastic Agents, Hormonal; D009570:Nitriles; D012709:Serum Albumin; D014230:Triazoles; D012710:Serum Albumin, Bovine
keywords: BSA; CD; FTIR; HSA; Spectroscopy