Corrigendum to “Exploring binding properties of sertraline with human serum albumin: Combination of spectroscopic and molecular modeling studies” [Chem. Biol. Interact. 242 (2015) 235–246]

Insights from a combination of theoretical and experimental methods for probing the biomolecular interactions between human serum albumin and clomiphene

“…A tryptophan residue (Trp214) is located in subdomain IIA of HSA. 20 The molecular docking results obtained using the AutoDock soware conrm the results of the experimental methods. As seen in the Fig.…”

“…Based on the available literature, we expect protein structural changes to correspond to a spectral shi in amide I (1650 cm À1 , mainly due to the C]O stretch) and amide II (1550 cm À1 , the C-N stretch coupled with N-H bending) bands. 20,44,45 An increase of the absorbance intensity for the protein amide I and amide II was observed in the spectra of the CLO-HSA complex. Both peaks of the protein are visible in both the presence and absence of CLO and they do not change in positions.…”

“…[17][18][19] Molecular dynamics (MD) simulation provides a detailed insight into protein-ligand complexes on the atomic scale. [19][20][21] This computational method allows the observation of alterations in the protein backbone structure or side chains upon interaction with a ligand. 22,23 Many studies have employed MD simulation for understanding the main protein-ligand binding interactions.…”

Investigating the interaction mechanism of fluorescent whitening agents to human serum albumin using saturation transfer difference-NMR, multi-spectroscopy, and docking studies

“…In the IR spectra of proteins, amides I and II are the most widely used vibrational bands for studying the conformation of protein secondary structures. 52 Amide I (1600-1700 cm À1 ) is primarily attributed to the C]O stretching vibration, whereas amide II (1500-1600 cm À1 ) is attributed to the coupling of the N-H in plane bending and C-N stretching modes. 53 As shown in Fig.…”

Enhancement of cell uptake and antitumor activity of selenadiazole derivatives through interaction and delivery by serum albumin

“…Especially, the binding affinity of drugs toward BSA and HSA affect the rate of the drug release to sites of catabolism or pharmacological action. 25 Generally, BSA is chosen as a target protein molecule due to its low cost, ready availability and unique ligand-binding properties. 26 The studies on drug's binding to BSA provide the information about structural features that could determine the therapeutic effectiveness of drugs, which become an important research eld in chemistry, life science and clinical medicine.…”