Abstract
Protein stability in ionic solution depends on the delicate balance between protein-ion and ion-ion interactions. To address the ion specific effects on the protein, we have examined the stability of myoglobin (Mb) in the presence of buffer and ammonium-based ionic liquids (ILs) (50%, v/v). Here, fluorescence and circular dichroism (CD) spectroscopy experiments are used to study the influence of ILs on structure and stability of Mb. Our experimental results reveal that more viscous ILs (sulphate or phosphate ions) are stabilizers and therefore more biocompatible for Mb structure. Surprisingly, the less viscous ILs such as acetate anion based ILs are destabilizers for the native structure of Mb. Our results explicitly elucidate that anion variation has significant influence on Mb stability efficiency than cation variation. This study provides insight into anion effects on protein stability and explains that the intrasolvent interactions can be leveraged to enhance the stability.
| Original language | English |
|---|---|
| Pages (from-to) | 114-123 |
| Number of pages | 10 |
| Journal | International Journal of Biological Macromolecules |
| Volume | 69 |
| DOIs | |
| Publication status | Published - Aug 2014 |
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All Science Journal Classification (ASJC) codes
- Structural Biology
- Biochemistry
- Molecular Biology
- Economics and Econometrics
- Energy(all)
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Variation in the structural changes of myoglobin in the presence of several protic ionic liquid. / Attri, Pankaj; Jha, Indrani; Choi, Eun Ha; Venkatesu, Pannuru.
In: International Journal of Biological Macromolecules, Vol. 69, 08.2014, p. 114-123.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Variation in the structural changes of myoglobin in the presence of several protic ionic liquid
AU - Attri, Pankaj
AU - Jha, Indrani
AU - Choi, Eun Ha
AU - Venkatesu, Pannuru
PY - 2014/8
Y1 - 2014/8
N2 - Protein stability in ionic solution depends on the delicate balance between protein-ion and ion-ion interactions. To address the ion specific effects on the protein, we have examined the stability of myoglobin (Mb) in the presence of buffer and ammonium-based ionic liquids (ILs) (50%, v/v). Here, fluorescence and circular dichroism (CD) spectroscopy experiments are used to study the influence of ILs on structure and stability of Mb. Our experimental results reveal that more viscous ILs (sulphate or phosphate ions) are stabilizers and therefore more biocompatible for Mb structure. Surprisingly, the less viscous ILs such as acetate anion based ILs are destabilizers for the native structure of Mb. Our results explicitly elucidate that anion variation has significant influence on Mb stability efficiency than cation variation. This study provides insight into anion effects on protein stability and explains that the intrasolvent interactions can be leveraged to enhance the stability.
AB - Protein stability in ionic solution depends on the delicate balance between protein-ion and ion-ion interactions. To address the ion specific effects on the protein, we have examined the stability of myoglobin (Mb) in the presence of buffer and ammonium-based ionic liquids (ILs) (50%, v/v). Here, fluorescence and circular dichroism (CD) spectroscopy experiments are used to study the influence of ILs on structure and stability of Mb. Our experimental results reveal that more viscous ILs (sulphate or phosphate ions) are stabilizers and therefore more biocompatible for Mb structure. Surprisingly, the less viscous ILs such as acetate anion based ILs are destabilizers for the native structure of Mb. Our results explicitly elucidate that anion variation has significant influence on Mb stability efficiency than cation variation. This study provides insight into anion effects on protein stability and explains that the intrasolvent interactions can be leveraged to enhance the stability.
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UR - http://www.scopus.com/inward/citedby.url?scp=84901478987&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2014.05.032
DO - 10.1016/j.ijbiomac.2014.05.032
M3 - Article
C2 - 24857872
AN - SCOPUS:84901478987
VL - 69
SP - 114
EP - 123
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
SN - 0141-8130
ER -