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Rosin Surfactant QRMAE Can Be Utilized as an Amorphous Aggregate Inducer: A Case Study of Mammalian Serum Albumin.

Ishtikhar M, Chandel TI, Ahmad A, Ali MS, Al-Lohadan HA, Atta AM, Khan RH - PLoS ONE (2015)

Bottom Line: It was observed that a suitable molar ratio of protein to QRMAE surfactant enthusiastically induces amorphous aggregate formation at a pH above two units of pI.Rosin surfactant QRMAE-albumins interactions revealed a unique interplay between the initial electrostatic and the subsequent hydrophobic interactions that play an important role towards the formation of hydrophobic interactions-driven amorphous aggregate.Amorphous aggregation of proteins is associated with varying diseases, from the formation of protein wine haze to the expansion of the eye lenses in cataract, during the expression and purification of recombinant proteins.

View Article: PubMed Central - PubMed

Affiliation: Protein Biophysics Laboratory, Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh - 202002, India.

ABSTRACT
Quaternary amine of diethylaminoethyl rosin ester (QRMAE), chemically synthesized biocompatible rosin based cationic surfactant, has various biological applications including its use as a food product additive. In this study, we examined the amorphous aggregation behavior of mammalian serum albumins at pH 7.5, i.e., two units above their isoelectric points (pI ~5.5), and the roles played by positive charge and hydrophobicity of exogenously added rosin surfactant QRMAE. The study was carried out on five mammalian serum albumins, using various spectroscopic methods, dye binding assay, circular dichroism and electron microscopy. The thermodynamics of the binding of mammalian serum albumins to cationic rosin modified surfactant were established using isothermal titration calorimetry (ITC). It was observed that a suitable molar ratio of protein to QRMAE surfactant enthusiastically induces amorphous aggregate formation at a pH above two units of pI. Rosin surfactant QRMAE-albumins interactions revealed a unique interplay between the initial electrostatic and the subsequent hydrophobic interactions that play an important role towards the formation of hydrophobic interactions-driven amorphous aggregate. Amorphous aggregation of proteins is associated with varying diseases, from the formation of protein wine haze to the expansion of the eye lenses in cataract, during the expression and purification of recombinant proteins. This study can be used for the design of novel biomolecules or drugs with the ability to neutralize factor(s) responsible for the aggregate formation, in addition to various other industrial applications.

No MeSH data available.


Related in: MedlinePlus

FT-IR spectra are showing Amide I and Amide II bands in the region of 1850–1250 cm-1 difference spectra of HSA in the absence and presence of QRMAE at pH below and above two unit of their pI.
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pone.0139027.g006: FT-IR spectra are showing Amide I and Amide II bands in the region of 1850–1250 cm-1 difference spectra of HSA in the absence and presence of QRMAE at pH below and above two unit of their pI.

Mentions: Amide I (1690–1620 cm-1) and amide II (1555–1535 cm-1) bands of IR spectra have been broadly used to characterize the chemical composition and conformational studies of proteins [47, 48]. So, we further examined the conformational alteration in amide I and II bands of HSA induced by cationic surfactant QRMAE by infrared spectroscopy. The presence of QRMAE chemical structure in the sample was confirmed by the appearance of the new broad absorption bands at 1618, 1442, 1407 and 1325 cm-1 and disappearance of 1755 cm-1 bands [32], as shown in Fig 6.


Rosin Surfactant QRMAE Can Be Utilized as an Amorphous Aggregate Inducer: A Case Study of Mammalian Serum Albumin.

Ishtikhar M, Chandel TI, Ahmad A, Ali MS, Al-Lohadan HA, Atta AM, Khan RH - PLoS ONE (2015)

FT-IR spectra are showing Amide I and Amide II bands in the region of 1850–1250 cm-1 difference spectra of HSA in the absence and presence of QRMAE at pH below and above two unit of their pI.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4587963&req=5

pone.0139027.g006: FT-IR spectra are showing Amide I and Amide II bands in the region of 1850–1250 cm-1 difference spectra of HSA in the absence and presence of QRMAE at pH below and above two unit of their pI.
Mentions: Amide I (1690–1620 cm-1) and amide II (1555–1535 cm-1) bands of IR spectra have been broadly used to characterize the chemical composition and conformational studies of proteins [47, 48]. So, we further examined the conformational alteration in amide I and II bands of HSA induced by cationic surfactant QRMAE by infrared spectroscopy. The presence of QRMAE chemical structure in the sample was confirmed by the appearance of the new broad absorption bands at 1618, 1442, 1407 and 1325 cm-1 and disappearance of 1755 cm-1 bands [32], as shown in Fig 6.

Bottom Line: It was observed that a suitable molar ratio of protein to QRMAE surfactant enthusiastically induces amorphous aggregate formation at a pH above two units of pI.Rosin surfactant QRMAE-albumins interactions revealed a unique interplay between the initial electrostatic and the subsequent hydrophobic interactions that play an important role towards the formation of hydrophobic interactions-driven amorphous aggregate.Amorphous aggregation of proteins is associated with varying diseases, from the formation of protein wine haze to the expansion of the eye lenses in cataract, during the expression and purification of recombinant proteins.

View Article: PubMed Central - PubMed

Affiliation: Protein Biophysics Laboratory, Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh - 202002, India.

ABSTRACT
Quaternary amine of diethylaminoethyl rosin ester (QRMAE), chemically synthesized biocompatible rosin based cationic surfactant, has various biological applications including its use as a food product additive. In this study, we examined the amorphous aggregation behavior of mammalian serum albumins at pH 7.5, i.e., two units above their isoelectric points (pI ~5.5), and the roles played by positive charge and hydrophobicity of exogenously added rosin surfactant QRMAE. The study was carried out on five mammalian serum albumins, using various spectroscopic methods, dye binding assay, circular dichroism and electron microscopy. The thermodynamics of the binding of mammalian serum albumins to cationic rosin modified surfactant were established using isothermal titration calorimetry (ITC). It was observed that a suitable molar ratio of protein to QRMAE surfactant enthusiastically induces amorphous aggregate formation at a pH above two units of pI. Rosin surfactant QRMAE-albumins interactions revealed a unique interplay between the initial electrostatic and the subsequent hydrophobic interactions that play an important role towards the formation of hydrophobic interactions-driven amorphous aggregate. Amorphous aggregation of proteins is associated with varying diseases, from the formation of protein wine haze to the expansion of the eye lenses in cataract, during the expression and purification of recombinant proteins. This study can be used for the design of novel biomolecules or drugs with the ability to neutralize factor(s) responsible for the aggregate formation, in addition to various other industrial applications.

No MeSH data available.


Related in: MedlinePlus