Macromolecular crowding induces molten globule state in the native myoglobin at physiological pH

Nasreen, Khalida; Ahamad, Shahzaib; Ahmad, Faizan; Hassan, Md. Imtaiyaz; Islam, Asimul

doi:10.1016/j.ijbiomac.2017.08.014

Cited by 40 publications

(32 citation statements)

References 90 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The presented results also indicate that both Mb and Hb form beta-sheet structures with a characteristic negative band near 218 nm and the positive band at 195 nm in CD spectra, which could be attributed to amyloid fibrils, in the presence of 45% of 2,2,2-trifluoroethanol (TFE) (black line). The data also collaborate analogous results indicating the formation of hemoglobin fibrils [28,40,41,59,60]. Nevertheless, when hydrogen sulfide is added, the CD spectra of both myoglobin and hemoglobin show 208 and 222 nm negative peaks typical for alpha-helical proteins (blue lines), suggesting the inhibition of fibrils by H 2 S.…”

Section: Hydrogen Sulfide Inhibition Of Myoglobin and Hemoglobin Fibrsupporting

confidence: 84%

“…Furthermore, Figures 5B and 6B also show CD the spectra of native Mb and Hb with clear minima at 208 and 222 nm characteristic for α-helix conformation of protein (red line). These negative peaks at 208 and 222 nm result from n → π* transition in the peptide bond of α-helical conformation [40,41,59,60]. The presented results also indicate that both Mb and Hb form beta-sheet structures with a characteristic negative band near 218 nm and the positive band at 195 nm in CD spectra, which could be attributed to amyloid fibrils, in the presence of 45% of 2,2,2-trifluoroethanol (TFE) (black line).…”

Section: Hydrogen Sulfide Inhibition Of Myoglobin and Hemoglobin Fibrmentioning

confidence: 58%

“…The results were expressed as the mean residue ellipticity. Data were corrected for buffer contributions [28,40,41].…”

Section: Circular Dichroism Spectroscopymentioning

confidence: 99%

See 2 more Smart Citations

Inhibition of Protein Fibrillation by Hydrogen Sulfide¹

Rosario-Alomar¹,

Quiñones-Ruiz²,

Kurouski³

et al. 2019

Amyloid Diseases

View full text Add to dashboard Cite

Amyloid fibrils are misfolded proteins, which are often associated with various neurodegenerative diseases such as Alzheimer's. The amount of hydrogen sulfide (H 2 S) is known to be reduced in the brain tissue of people diagnosed with Alzheimer's disease relative to that of healthy individuals. Hen Egg-White Lysozyme (HEWL) forms typical β-sheet-rich fibrils during 70 minutes at low pH and high temperatures. These results are consistent with the ThT findings that β-sheets structure is also present in myoglobin (Mb), and hemoglobin (Hb) in the presence of 45% TFE. The addition of H 2 S in the process completely inhibits the formation of amyloid fibrils in HEWL, Mb, and Hb as revealed by several spectroscopic techniques. Non-resonance Raman bands corresponding to disulfide (RSSR) vibrational modes in the 550-500 cm-1 spectral range decreases in intensity and is accompanied by the appearance of a new 490 cm-1 band assigned to the trisulfide group (RSSSR). Intrinsic tryptophan fluorescence shows a partial denaturation of HEWL containing trisulfide bonds. Overall, the Mb and Hb result ties excellent with the HEWL data showing that the presence of H 2 S during these proteins fibrillation processes protects the α-helical protein structures, preventing the formation of amyloids in these different proteins moieties.

show abstract

Section: Hydrogen Sulfide Inhibition Of Myoglobin and Hemoglobin Fibrsupporting

confidence: 84%

Section: Hydrogen Sulfide Inhibition Of Myoglobin and Hemoglobin Fibrmentioning

confidence: 58%

See 1 more Smart Citation

Inhibition of Protein Fibrillation by Hydrogen Sulfide¹

Rosario-Alomar¹,

Quiñones-Ruiz²,

Kurouski³

et al. 2019

Amyloid Diseases

View full text Add to dashboard Cite

show abstract

“…Binding free energy released on interaction of Mb and dextran dimer on docking was calculated to be −2.5 kcal/mol, indicates favorable interactions between Mb and dextran dimer. The type of interaction between ficoll 70 and Mb was already reported where molecular docking was performed using AutoDock4 software [46]. In silico studies had showed that notable interaction existed between Mb and ficoll 70 [46].…”

Section: Molecular Docking Studiesmentioning

confidence: 95%

“…Earlier, we have reported that ficoll 70 binds with Mb [46]. To know whether dextran 70 also binds to Mb; and to delineate the chemical basis of structural changes in Mb due to dextran 70, isothermal titration calorimetry (ITC) was carried out to find out possible binding between Mb and dextran 70.…”

Section: Isothermal Titration Calorimetry Measurementsmentioning

confidence: 99%

Interactions Under Crowding Milieu: Chemical-Induced Denaturation of Myoglobin is Determined by the Extent of Heme Dissociation on Interaction with Crowders

et al. 2020

Self Cite

View full text Add to dashboard Cite

Generally, in vivo function and structural changes are studied by probing proteins in a dilute solution under in vitro conditions, which is believed to be mimicking proteins in intracellular milieu. Earlier, thermal-induced denaturation of myoglobin, in the milieu of crowder molecule showed destabilization of the metal protein. Destabilization of protein by thermal-induced denaturation involves a large extrapolation, so, the reliability is questionable. This led us to measure the effects of macromolecular crowding on its stability by chemical-induced denaturation of the protein using probes like circular dichroism and absorption spectroscopy in the presence of dextran 70 and ficoll 70 at various pHs (acidic: 6.0, almost neutral: 7.0 and basic: 8.0). Observations showed that the degree of destabilization of myoglobin was greater due to ficoll 70 as compared to that of dextran 70 so it can be understood that the nature of the crowder or the shape of the crowder has an important role towards the stability of proteins. Additionally, the degree of destabilization was observed as pH dependent, however the pH dependence is different for different crowders. Furthermore, isothermal titration calorimetry and molecular docking studies confirmed that both the crowders (ficoll and dextran) bind to heme moiety of myoglobin and a single binding site was observed for each.

show abstract

Biological Implications of Polyethylene Glycol and PEGylation: Therapeutic Approaches Based on Biophysical Studies and Protein Structure-Based Drug Design Tools

Raina

Singh

Islam

2021

Innovations and Implementations of Computer Aided Drug Discovery Strategies in Rational Drug Design

View full text Add to dashboard Cite

Macromolecular crowding induces molten globule state in the native myoglobin at physiological pH

Cited by 40 publications

References 90 publications

Inhibition of Protein Fibrillation by Hydrogen Sulfide¹

Inhibition of Protein Fibrillation by Hydrogen Sulfide¹

Interactions Under Crowding Milieu: Chemical-Induced Denaturation of Myoglobin is Determined by the Extent of Heme Dissociation on Interaction with Crowders

Biological Implications of Polyethylene Glycol and PEGylation: Therapeutic Approaches Based on Biophysical Studies and Protein Structure-Based Drug Design Tools

Contact Info

Product

Resources

About

Macromolecular crowding induces molten globule state in the native myoglobin at physiological pH

Cited by 40 publications

References 90 publications

Inhibition of Protein Fibrillation by Hydrogen Sulfide1

Inhibition of Protein Fibrillation by Hydrogen Sulfide1

Interactions Under Crowding Milieu: Chemical-Induced Denaturation of Myoglobin is Determined by the Extent of Heme Dissociation on Interaction with Crowders

Biological Implications of Polyethylene Glycol and PEGylation: Therapeutic Approaches Based on Biophysical Studies and Protein Structure-Based Drug Design Tools

Contact Info

Product

Resources

About

Inhibition of Protein Fibrillation by Hydrogen Sulfide¹

Inhibition of Protein Fibrillation by Hydrogen Sulfide¹