Commentary on "Spectral characterization of the binding and conformational changes of serum albumins upon interaction with an anticancer drug, anastrozole"

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2015

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Pergamon-elsevier Science Ltd

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Physics Group
Atılım University Physics Division was established with the purpose of educating the first-year students of the Engineering and other Departments by providing the general physics courses and, in addition, to make scientific and technological researches at the universal level. Now adays, Physics Division provide the students of Engineering, School of Aviation and Mathematics Departments with the general physics lectures having international education quality. We have in the Group the facilities of the mechanics and electricity laboratories, where the students have the opportunity to realize the practice of the theoretical knowledge in physics. Beside the compulsory courses (General Physics I and General Physics II) there are also elective courses offered by the Group. The faculty members in the Group, whose research interests and fields are given in web-page of the Group in details, perform theoretical as well as experimental researches and make publications in SSC-index journals. Graduate program, with master of sciences and doctorate degree courses and theses, is offered in different scientific areas (for details, see the web-page of the Division). In the Physcis Division there are 6 faculty members, five research assistants, and one technician.

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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 FUR experiments. (C) 2014 Elsevier B.V. All rights reserved.

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Korkmaz, Filiz/0000-0003-3512-3521

Keywords

HSA, BSA, Spectroscopy, FTIR, CD

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1

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Q1

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Volume

138

Issue

Start Page

967

End Page

968

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