Effect of the sugar and polyol additives on the aggregation kinetics of BSA in the presence of N-cetyl-N,N,N-trimethyl ammonium bromide

Sharma, Anurag; Pasha, Javeed M.; Deep, Shashank

doi:10.1016/j.jcis.2010.06.054

Cited by 32 publications

(18 citation statements)

References 43 publications

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“…The longitudinal LSPR is becoming closer to the same band of pure GNRs as the BSA concentration increases. The origin of this can be the fact that a strong excess of BSA in the presence of CTAB is known to form aggregates of proteins [27]. The concentration of BSA actually interacting with GNRs is thus much lower than the nominal concentration.…”

Section: Discussionmentioning

confidence: 99%

Study of gold nanorods–protein interaction by localized surface plasmon resonance spectroscopy

et al. 2013

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In this paper, gold nanorods' (GNRs) interaction with different proteins (i.e. carbonic anhydrase, lysozyme, ovalbumin and bovine serum albumin (BSA)) at physiological pH is investigated using localized surface plasmon resonance (LSPR) spectroscopy. We observe that the incubation of these proteins at different concentrations with cetyltrimethylammonium bromidecapped GNRs of three aspect ratios induces dramatic changes in the extinction spectra of the nanoparticles. In particular, we correlate the position and shape of the longitudinal LSPR peaks to the ability of the proteins to specifically interact with GNRs' surface. The different types of behaviour observed are explained by the exposed molecular surface area of the proteins' cysteine residues as modelled on the basis of their respective X-ray crystallographic data structures. Cysteine is the only amino acid that exhibits an SH group that is well known to have a strong affinity to gold. The presence and the accessibility of such a residue may explain the protein binding to GNRs. The isoelectric point of the proteins is also an important characteristic to take into account, as the electrostatic strength between GNRs and protein explains some of the cases where aggregates are formed.

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Section: Discussionmentioning

confidence: 99%

Study of gold nanorods–protein interaction by localized surface plasmon resonance spectroscopy

et al. 2013

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“…Protein aggregation is the phenomenon of generic propensity among proteins, and its exact mechanism is still not deciphered. This phenomenon is involved in breaking the cellular quality-control mechanism and is associated with a number of human diseases such as Alzheimer’s disease, Parkinson’s disease, prion diseases (bovine spongiform encephalopathy and Creutzfeldt–Jakob disease), amyotrophic lateral sclerosis, Huntington’s disease, Down’s syndrome, cataract, and sickle cell disease. , These diseases are also referred to as proteopathies or proteinopathies, protein conformational disorders, or protein misfolding diseases . According to some recent reports of 2019, the world’s suffering from Alzheimer’s disease is 50 million, while that from Parkinson’s disease is 10 million .…”

Section: Introductionmentioning

confidence: 99%

Heparin Accelerates the Protein Aggregation via the Downhill Polymerization Mechanism: Multi-Spectroscopic Studies to Delineate the Implications on Proteinopathies

et al. 2021

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Heparin is one of the members of the glycosaminoglycan (GAG) family, which has been associated with protein aggregation diseases including Alzheimer’s disease, Parkinson’s disease, and prion diseases. Here, we investigate heparin-induced aggregation of bovine serum albumin (BSA) using different spectroscopic techniques [absorption, 8-anilino-1-naphthalene sulfonic acid (ANS) and thioflavin T (ThT) fluorescence binding, and far- and near-UV circular dichroism]. Kinetic measurements revealed that heparin is involved in the significant enhancement of aggregation of BSA. The outcomes showed dearth of the lag phase and a considerable change in rate constant, which provides conclusive evidence, that is, heparin-induced BSA aggregation involves the pathway of the downhill polymerization mechanism. Heparin also causes enhancement of fluorescence intensity of BSA significantly. Moreover, heparin was observed to form amyloids and amorphous aggregates of BSA which were confirmed by ThT and ANS fluorescence, respectively. Circular dichroism measurements exhibit a considerable change in the secondary and tertiary structure of the protein due to heparin. In addition, binding studies of heparin with BSA to know the cause of aggregation, isothermal titration calorimetry measurements were exploited, from which heparin was observed to promote the aggregation of BSA by virtue of electrostatic interactions between positively charged amino acid residues of protein and negatively charged groups of GAG. The nature of binding of heparin with BSA is very much apparent with an appreciable heat of interaction and is largely exothermic in nature. Moreover, the Gibbs free energy change (ΔG) is negative, which indicates spontaneous nature of binding, and the enthalpy change (ΔH) and entropy change (ΔS) are also largely negative, which suggest that the interaction is driven by hydrogen bonding.

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“…Changes in the absorbance can be attributed to the scattering due to the protein solution turbidity [13,38,39].…”

Section: Od Measurementsmentioning

confidence: 99%

Early stage aggregation of human serum albumin in the presence of metal ions

Stirpe

Pantusa

Rizzuti

et al. 2011

International Journal of Biological Macromolecules

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Effect of the sugar and polyol additives on the aggregation kinetics of BSA in the presence of N-cetyl-N,N,N-trimethyl ammonium bromide

Cited by 32 publications

References 43 publications

Study of gold nanorods–protein interaction by localized surface plasmon resonance spectroscopy

Study of gold nanorods–protein interaction by localized surface plasmon resonance spectroscopy

Heparin Accelerates the Protein Aggregation via the Downhill Polymerization Mechanism: Multi-Spectroscopic Studies to Delineate the Implications on Proteinopathies

Early stage aggregation of human serum albumin in the presence of metal ions

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