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Editorial Citation - WoS: 1Citation - Scopus: 1Commentary on "spectral Characterization of the Binding and Conformational Changes of Serum Albumins Upon Interaction With an Anticancer Drug, Anastrozole"(Pergamon-elsevier Science Ltd, 2015) Korkmaz, FilizThe 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.Article Citation - WoS: 17Citation - Scopus: 18in Situ Opening/Closing of Ompg From e. coli and the Splitting of Β-Sheet Signals in Atr-Ftir Spectroscopy(Pergamon-elsevier Science Ltd, 2012) Korkmaz, Filiz; Koester, Stefan; Yildiz, Oezkan; Maentele, Werner; Mäntele, Werner; Köster, StefanThe pH dependent opening and closure of Escherichia coli OmpG is driven by the formation and breaking of hydrogen bridges in beta-strands S11-S13. We have investigated the in situ secondary structural changes of OmpG with ATR-FTIR difference spectroscopy in order to detect the signals associated with the newly established interactions. Curve-fitting of OmpG in two pH conditions revealed the splitting and shifting of beta-sheet signals upon opening of the channel. Besides secondary structure changes, there are also amino acid side chain signals that play active role in opening/closing of the channel. An interaction among positively charged arginines and negatively charged aspartic and glutamic acid residues is suggested upon closure of the channel while this interaction is abolished when the channel opens at higher pH. (C) 2012 Elsevier B.V. All rights reserved.
