Influence of protic ionic liquids on the structure and stability of succinylated Con A

Attri, Pankaj; Venkatesu, Pannuru

doi:10.1016/j.ijbiomac.2012.04.017

Cited by 37 publications

(30 citation statements)

References 44 publications

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“…The tertiary structure of CT was monitored by using near-UV (250-300 nm) (1.0 cm path length cuvette). Each sample spectrum was obtained by subtracting the appropriate blank media (without CT) from the experimental spectrum and was 30 collected by averaging six spectra. (http://www.molegro.com) with the default parameter settings.…”

Section: Methodsmentioning

confidence: 99%

“…The estimated diameter from the X-ray crystallographic (Protein Data Bank (PDB) code 2CHA) structure of the CT is 4.4 nm. 43 30 The content of hydrophobic and polar amino acid groups in the primary structure of CT is around 48 % and 52 %, respectively. 44 CT is folded into two anti-parallel β-barrel domains followed by an anti-parallel hairpin motif with small α-helix content.…”

Section: Introductionmentioning

confidence: 99%

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A comparative study of the effects of the Hofmeister series anions of the ionic salts and ionic liquids on the stability of α-chymotrypsin

2015

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In this article, we have compared the anions of sodium salts (Is) and ionic liquids (ILs) with the stability and structure of αchymotrypsin (CT), through fluorescence, thermal fluorescence 10 analysis and circular dichroism (CD) spectroscopy. The experimental results revealed that the Hofmeister series of anions such as SCN‾, SO 4 2¯, Cl‾, Br‾, CH 3 COO‾ and I‾ of Is destabilized the native structure of the CT. On the contrary, the anions such as CH 3 COO‾, Cl‾ and Br‾ of imidazolium-based IL with fixed cation 15 such as 1-butyl-3-methylimidazolium, [Bmim] + stabilized the native structure of the CT. The remaining anions of ILs such as SCN‾, HSO 4 ‾, and I‾ acted as denaturing agents for the native structure of CT. Furthermore, molecular docking results show that the imidazolium-cation of the IL enters the sub-domains of 20 the CT and interacts with the ionic residues of the CT, that is Ser217 close to Trp215. This interaction is in well agreement with the fluorescence quenching observed for CT in the presence of [Bmim] + . On the other hand, the destabilizing anion such as SO 4 2¯w as observed to be directly interacting with Ser195 in the 25 active site of the CT. We have observed that the Hofmeister series effects of anions of either Is or ILs are entirely based on the interaction of the anions with its counterion, that is the cation, with solvent molecules, as well as with the protein surface. Evidently, these interactions vary with co-solvent system and the 30 type of the protein. Hence, the stability of a biomolecule in the presence of the anions may or may not obey Hofmeister series. 65 80

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A comparative study of the effects of the Hofmeister series anions of the ionic salts and ionic liquids on the stability of α-chymotrypsin

2015

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“…For this series, the trimethylammonium PILs followed the expected behavior according to the Hofmeister series based on the kosmotropicity of the anions. 410 In contrast, an investigation into the ability of PILs to inhibit amyloid fibril formation of lysozyme used a series of PILs as additives, which consisted of the tetramethylguinidium cation paired with formate, acetate, trifluoroacetate, trifluoromethanesulfonate, tetrafluoroborate, nitrate, chloride, and perchlorate anions. No trend was identified between the ability of the PILs to inhibit fibril formation and the anionic extent of kosmotropicity.…”

Section: Protein Stabilizationmentioning

confidence: 99%

Protic Ionic Liquids: Evolving Structure–Property Relationships and Expanding Applications

2015

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“…The percentage ratio of S values of IPAF to MeCN is 89%, similar to the ratio of tryptophan peak heights of IPAF to MECN measured from S1 as 82%. This is expected since tryptophan has a higher quantum yield in a more hydrophobic solvent environment as compared to a hydrophilic environment [48]. …”

Section: Resultsmentioning

confidence: 99%

“…For example, the protic ionic liquid triethylammonium dihydrogen phosphate has been shown to effectively stabilize succinylated concanavalin A, a protein with four monomeric units in a folded jelly roll motif [48]. For IPAF, the formate ion should be considered to be a kosmotropic or “structure-making” anion while the isopropylammonium ion is more of a chaotropic cation.…”

Section: Resultsmentioning

confidence: 99%

The ionic liquid isopropylammonium formate as a mobile phase modifier to improve protein stability during reversed phase liquid chromatography

Zhou

Danielson

2013

Journal of Chromatography B

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The room temperature ionic liquid isopropylammonium formate (IPAF) is studied as a reversed phase HPLC mobile phase modifier for separation of native proteins using a polymeric column and this protein stability is compared to that using acetonitrile (MeCN) as the standard organic mobile phase modifier. A variety of important proteins with different numbers of subunits is investigated, including non-subunit proteins: albumin, and amyloglucosidase (AMY); a two subunit protein: thyroglobulin (THY); and four subunit proteins: glutamate dehydrogenase (GDH) and lactate dehydrogenase (LDH). A significant enhancement in protein stability is observed in the chromatograms upon using IPAF as a mobile phase modifier. The first sharper peak at about 2 min represented protein in primarily the native form and a second broader peak more retained at about 5–6 min represented substantially denatured or possibly aggregated protein. The investigated proteins (except LDH) could maintain the native form within up to 50% IPAF, while a mobile phase, with as low as 10% MeCN, induced protein denaturation. The assay for pyruvate using LDH has further shown that enzymatic activity can be maintained up to 30% IPAF in water in contrast to no activity using 30% MeCN.

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Influence of protic ionic liquids on the structure and stability of succinylated Con A

Cited by 37 publications

References 44 publications

A comparative study of the effects of the Hofmeister series anions of the ionic salts and ionic liquids on the stability of α-chymotrypsin

A comparative study of the effects of the Hofmeister series anions of the ionic salts and ionic liquids on the stability of α-chymotrypsin

Protic Ionic Liquids: Evolving Structure–Property Relationships and Expanding Applications

The ionic liquid isopropylammonium formate as a mobile phase modifier to improve protein stability during reversed phase liquid chromatography

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