The Combination of Organic Anions With Serum Albumin

Duggan, Edward L.; Luck, J. Murray

doi:10.1016/s0021-9258(18)35630-8

Cited by 68 publications

(18 citation statements)

References 14 publications

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“…Interestingly, the coexistence of SDS behaves to protect the HSA structure in urea solutions. This phenomenon was first observed by Duggan and Luck in 1948 as a prevention of rise in viscosity in albumin−urea solutions upon the addition of certain organic anions . They found that SDS was most effective in the anions they studied.…”

Section: Discussionmentioning

confidence: 65%

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Re-formation of the Helical Structure of Human Serum Albumin by the Addition of Small Amounts of Sodium Dodecyl Sulfate after the Disruption of the Structure by Urea. A Comparison with Bovine Serum Albumin

and

Takeda

1999

Langmuir

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Upon the addition of small amounts of sodium dodecyl sulfate (SDS), the helicity of human serum albumin (HSA), lost in the urea denaturation, was mostly recovered. The profile of the recovery differed depending on the urea concentration. Then the urea concentrations were divided into three ranges: [1] a range below 3 M where the helicity only decreased as in the absence of urea (the helicity decreased down to 49% in the SDS solution); [2] a range between 4 and 8 M where the helicity initially increased up to 66% (this was the same as in the native state) and then sharply decreased; [3] a range above 9 M where the helicity only increased with an increase in added SDS concentration. When SDS was added prior to the urea denaturation, the same helicity was obtained at each surfactant concentration. Thus the SDS denaturation finally predominates over the urea denaturation. In the middle range, profiles of the structural change were rather complicated. The increase and decrease of helicity were accomplished below 3 mM SDS. It is worth noting that the helicity is recovered upon the addition of SDS less than 300 µM in the second range except for 8 M urea ([HSA] ) 10 µM). The helicity-recovery profile of HSA differs from that of a homologous protein, bovine serum albumin, the helicity of which recovers to some degree, but not completely. This difference might be attributed to the fact that the C-terminal helical-rod of HSA is amphiphilic, while that of bovine serum albumin is hydrophobic as a whole.

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Section: Discussionmentioning

confidence: 65%

“…Just half a century ago, Duggan and Luck observed that certain organic anions prevented the rise in viscosity of serum albumins by urea . They found that sodium dodecyl sulfate (SDS) was most effective in the anions they studied.…”

Section: Introductionmentioning

confidence: 99%

Re-formation of the Helical Structure of Human Serum Albumin by the Addition of Small Amounts of Sodium Dodecyl Sulfate after the Disruption of the Structure by Urea. A Comparison with Bovine Serum Albumin

and

Takeda

1999

Langmuir

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“…We would like to note here that it has been shown that some specific ligands such as polymers, surfactants, etc. can alter the protein–ligand binding mode in particular and mechanism of binding events in general. − Therefore, it will be interesting to look at the outcomes of the protein–NCs binding event if the interaction of protein is done with NCs modified with such type of ligands.…”

Section: Introductionmentioning

confidence: 99%

Probing the Interaction of Bovine Serum Albumin with Copper Nanoclusters: Realization of Binding Pathway Different from Protein Corona

et al. 2021

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With an aim to understand the interaction mechanism of bovine serum albumin (BSA) with copper nanoclusters (CuNCs), three different types CuNCs having chemically different surface ligands, namely, tannic acid (TA), chitosan, and cysteine (Cys), have been fabricated, and investigations are carried out in the absence and presence of protein (BSA) at ensemble-averaged and single-molecule levels. The CuNCs, capped with different surface ligands, are consciously chosen so that the role of surface ligands in the overall protein− NCs interactions is clearly understood, but, more importantly, to find whether these CuNCs can interact with protein in a new pathway without forming the "protein corona", which otherwise has been observed in relatively larger nanoparticles when they are exposed to biological fluids. Analysis of the data obtained from fluorescence, ζ-potential, and ITC measurements has clearly indicated that the BSA protein in the presence of CuNCs does not attain the binding stoichiometry (BSA/CuNCs > 1) that is required for the formation of "protein corona". This conclusion is further substantiated by the outcome of the fluorescence correlation spectroscopy (FCS) study. Further analysis of data and thermodynamic calculations have revealed that the surface ligands of the CuNCs play an important role in the protein−NCs binding events, and they can alter the mode and thermodynamics of the process. Specifically, the data have demonstrated that the binding of BSA with TA-CuNCs and Chitosan-CuNCs follows two types of binding modes; however, the same with Cys-CuNCs goes through only one type of binding mode. Circular dichroism (CD) measurements have indicated that the basic structure of BSA remains almost unaltered in the presence of CuNCs. The outcome of the present study is expected to encourage and enable better application of NCs in biological applications.

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“…In addition to the methodologies mentioned above, proteins can unfold in response to surfactants and drug molecules. [14][15][16][17][18][19][20][21][22][23][24][25] At a high surfactant concentration, the three dimensional structure of a protein is destroyed and the protein is said to be denatured. However, in 1948 Duggan and Luck 23 showed that the urea induced denaturation of proteins may be prevented by the addition of a small amount of SDS.…”

Section: Introductionmentioning

confidence: 99%

“…[14][15][16][17][18][19][20][21][22][23][24][25] At a high surfactant concentration, the three dimensional structure of a protein is destroyed and the protein is said to be denatured. However, in 1948 Duggan and Luck 23 showed that the urea induced denaturation of proteins may be prevented by the addition of a small amount of SDS. Moriyama and Takeda 19a proposed that the secondary structure of HSA remains more or less unchanged up to the addition of 200 mM of SDS.…”

Section: Introductionmentioning

confidence: 99%

Protein unfolding and subsequent refolding: a spectroscopic investigation

Anand

Jash

Mukherjee

2011

Phys. Chem. Chem. Phys.

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The mechanism by which the protein Bovine Serum Albumin (BSA) undergoes unfolding induced by Guanidine Hydrochloride (GdHCl) and then the subsequent refolding brought in by many-fold dilution was studied by steady-state fluorescence, anisotropy, time resolved measurements and Circular Dichroism (CD) spectroscopy. CD data reveal that the protein attains a degree of extra rigidity at low concentrations of the denaturant, GdHCl, and this observation was correlated with other techniques used in this present work. The unfolding and refolding of BSA appear to proceed through intermediates and both the processes are sequential in nature. The intrinsic fluorescence from the tryptophan amino acid residue of BSA and another external fluorophore Nile Red was made use of in order to investigate the mechanisms of unfolding and refolding and we have conclusively proved that both these processes follow a reversible mechanism.

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The Combination of Organic Anions With Serum Albumin

Cited by 68 publications

References 14 publications

Re-formation of the Helical Structure of Human Serum Albumin by the Addition of Small Amounts of Sodium Dodecyl Sulfate after the Disruption of the Structure by Urea. A Comparison with Bovine Serum Albumin

Re-formation of the Helical Structure of Human Serum Albumin by the Addition of Small Amounts of Sodium Dodecyl Sulfate after the Disruption of the Structure by Urea. A Comparison with Bovine Serum Albumin

Probing the Interaction of Bovine Serum Albumin with Copper Nanoclusters: Realization of Binding Pathway Different from Protein Corona

Protein unfolding and subsequent refolding: a spectroscopic investigation

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