Polyphosphate binding interactions with bovine serum albumin in protein-polyphosphate precipitates

1981 ◽  
Vol 29 (3) ◽  
pp. 536-539 ◽  
Author(s):  
Vaughn Vandegrift ◽  
Robert R. Evans
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Interactions

Spectroscopic Studies of Binding interactions of 2-Chloroethylphenyl Sulphide with Bovine Serum Albumin

2021 ◽  
pp. 117144
Author(s):  
Afreen Jahan Rahman ◽  
Lajpreet Kaur ◽  
Mallika Pathak ◽  
Anju Singh ◽  
Piyush Verma ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Studies ◽  
Binding Interactions

scholarly journals Synthesis of acetamide derivatives of 1,2,4-triazole bearing azinane and their binding interactions with bovine serum albumin using spectroscopic techniques

2018 ◽  
Vol 42 (6) ◽  
pp. 1459-1478
Author(s):  
Javed IQBAL ◽  
Aziz UR-REHMAN ◽  
Muhammad Athar ABBASI ◽  
Sabahat Zahra SIDDIQUI ◽  
Hira KHALID ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Techniques ◽  
Binding Interactions ◽  
Derivatives Of

Binding interactions of water-soluble camptothecin derivatives with bovine serum albumin

2012 ◽  
Vol 86 ◽  
pp. 124-130 ◽  
Author(s):  
Qingyong Li ◽  
Qiaochu Zhu ◽  
Xiaoqiu Deng ◽  
Wuna He ◽  
Tengfei Zhao ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Water Soluble ◽  
Binding Interactions

scholarly journals FT-IR Spectroscopy for the Identification of Binding Sites and Measurements of the Binding Interactions of Important Metal Ions with Bovine Serum Albumin

2019 ◽  
Vol 87 (1) ◽  
pp. 5 ◽  
Author(s):  
Hassan Alhazmi
Keyword(s):  
Bovine Serum Albumin ◽  
Ir Spectroscopy ◽  
Serum Albumin ◽  
Metal Ions ◽  
Bovine Serum ◽  
Metal Ion ◽  
Binding Interaction ◽  
Binding Interactions ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

Proteins play crucial roles in the transportation and distribution of therapeutic substances, including metal ions in living systems. Some metal ions can strongly associate, while others show low affinity towards proteins. Consequently, in the present work, the binding behaviors of Ca2+, Ba2+, Ag+, Ru3+, Cu2+ and Co2+ with bovine serum albumin (BSA) were screened. BSA and the metal ions were allowed to interact at physiological pH and their binding interactions were screened by using FT-IR spectroscopy. Spectra were collected by using hydrated films over a range of 4000–400 cm−1. The interaction was demonstrated by a significant reduction in the spectral intensities of the amide I (C=O stretching) and amide II bands (C–N stretching coupled to NH bending) of the protein after complexation with metal ions. The binding interaction was further revealed by spectral shifting of the amide I band from 1651 cm−1 (free BSA) to 1653, 1654, 1649, 1655, 1655, and 1654 cm−1 for BSA–Ca2+, BSA–Ba2+, BSA–Ag+, BSA–Ru3+, BSA–Cu2+ and BSA–Co2+ complexes, respectively. The shifting of the amide I band was due to the interactions of metal ions with the O and N atoms of the ligand protein. Estimation of the secondary protein structure showed alteration in the protein conformation, characterized by a marked decrease (12.9–40.3%) in the α-helix accompanied by increased β-sheet and β-turn after interaction with the metal ions. The interaction results of this study were comparable with those reported in our previous investigation of metal ion–BSA interactions using affinity capillary electrophoresis (ACE), which has proven the accuracy of the FT-IR technique in the measurement of interactions between proteins and metal ions.

scholarly journals Binding interactions and FRET between bovine serum albumin and various phenothiazine-/anthracene-based dyes: a structure–property relationship

RSC Advances ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 1679-1693
Author(s):  
Shouvik Bhuin ◽  
Sayantan Halder ◽  
Subit Kumar Saha ◽  
Manab Chakravarty
Keyword(s):  
Energy Transfer ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Structure Property ◽  
Binding Interactions ◽  
Property Relationship ◽  
Structure Property Relationship

The present study demonstrates binding interactions and Förster resonance energy transfer (FRET) between bovine serum albumin (BSA) and a series of structurally and electronically diverse phenothiazine (PTZ) and anthracene (ANT) dyes.

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