[NMR paper] Selective binding and dynamics of imidazole alkyl sulfate ionic liquids with human serum albumin and collagen - a detailed NMR investigation.
Abstract
The interaction of ionic liquid (IL) with protein is now becoming important as it stabilizes the protein due to the selective cation-anion combination of the IL. The binding and dynamics of the green solvents such as imidazole alkyl sulfate based ILs, viz., 1-butyl-3-methylimidazolium alkyl [where alkyl = hydrogen, methyl, octyl and dodecyl] sulfate, with two distinct model proteins, namely human serum albumin (HSA) and collagen in aqueous solution, have been investigated with the aid of solution nuclear magnetic resonance (NMR). Interactions of ILs with HSA and collagen have been probed at the atomistic level through NMR determined parameters, such as 1H line-shapes, selective and non-selective spin-lattice relaxation times (T1SEL & T1NS) and spin-spin relaxation times (T2). Furthermore, saturation transfer difference (STD) NMR has been used to monitor the spatial proximities of ILs with HSA and collagen. The results indicate that despite the type of protein (HSA or collagen), STD NMR of protein-IL mixtures exhibits responses only from the anionic part of the selected ILs. Also, a combination of T1SEL and T1NS measurements indicates the genuine protein-IL interaction. Furthermore, it was observed that the global binding affinity between IL and proteins is enhanced with an increase in alkyl chain length of the anionic portion of the IL. The present study thus highlights the role of the anionic part of ILs in the interaction with the selected proteins. The outcome of the present study provides an opportunity to design new ILs with a judicious choice of anionic and cationic parts for targeted functionalities.
PMID: 29560969 [PubMed - as supplied by publisher]
[NMR paper] Allosteric Sensing of Fatty Acid Binding by NMR: Application to Human Serum Albumin.
Allosteric Sensing of Fatty Acid Binding by NMR: Application to Human Serum Albumin.
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J Med Chem. 2016 Aug 25;59(16):7457-65
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[NMR paper] Mn(II) binding to human serum albumin: a ¹H-NMR relaxometric study.
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Abstract
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DEER in Biological Multispin-Systems: A Case Study on the Fatty Acid Binding to Human Serum Albumin
DEER in Biological Multispin-Systems: A Case Study on the Fatty Acid Binding to Human Serum Albumin
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 10 March 2011</br>
Matthias J.N., Junk , Hans W., Spiess , Dariush, Hinderberger</br>
In this study, self-assembled systems of human serum albumin (HSA) and spin-labeled fatty acids are characterized by double electron–electron resonance (DEER). HSA, being the most important transport protein of the human blood, is capable to host up to seven paramagnetic fatty acid...
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[NMR paper] Analysis of competitive binding of ligands to human serum albumin using NMR relaxatio
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The competitive binding of two ligands, ibuprofen (IBP) and salicylic acid (SAL), to human serum albumin (HSA) was studied by using nuclear magnetic resonance (NMR) relaxation measurements. When the concentration of one ligand was...
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[NMR paper] The binding of 5-fluorouracil to native and modified human serum albumin: UV, CD, and
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[NMR paper] 13C NMR studies of the binding of medium-chain fatty acids to human serum albumin.
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Authors: Kenyon MA, Hamilton JA
Binding of the medium-chain fatty acids (MCFA), octanoic (OCT) and decanoic (DEC) acid, to human serum albumin (HSA) has been studied by 13C NMR spectroscopy. NMR spectra at 35 degrees C showed an apparently homogeneous binding environment (a single, narrow resonance for the 13C-enriched carboxyl...
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[NMR paper] 13C NMR studies of the binding of medium-chain fatty acids to human serum albumin.
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Binding of the medium-chain fatty acids (MCFA), octanoic (OCT) and decanoic (DEC) acid, to human serum albumin (HSA) has been studied by 13C NMR spectroscopy. NMR spectra at 35 degrees C showed an apparently homogeneous binding environment (a single, narrow resonance for the 13C-enriched carboxyl...
Selective binding and dynamics of imidazole alkyl sulfate ionic liquids with human serum albumin and collagen - a detailed NMR investigation.
Linear Mode
