Acetonitrile-induced unfolding of porcine pepsin A

Cardoso, Teresa; Oliveira, Cybelle Pereira de; Sarmento, Ana Cristina; Pereira, Anabela; Nutley, Margaret; Jess, Thomas J.; Kelly, Sharon M.; Cooper, Alan; Price, Nicholas C.; Pires, Euclides; Barros, Marlene

doi:10.1016/j.ijbiomac.2009.05.006

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Cited by 10 publications

(1 citation statement)

References 59 publications

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“…Various non-native states of proteins and polypeptides are easily obtained by introducing organic solvent as a co-solvent. For example, alcohols are extensively used as a co-solvent that modifies the native conformation of protein [6,7]. Fluorinated alcohols such as 2,2,2-trifluorethanol (TFE) and 1,1,1,3,3,3-hexafluoro-isopropanol (HFIP) are extensively used to study the conformation of proteins or peptides in the monomeric state [8,9].…”

Section: Introductionmentioning

confidence: 99%

Ethanol and acetonitrile induces conformational changes in porcine pepsin at alkaline denatured state

Shanmugam

Selvi

Mandal

2012

International Journal of Biological Macromolecules

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Section: Introductionmentioning

confidence: 99%

Ethanol and acetonitrile induces conformational changes in porcine pepsin at alkaline denatured state

Shanmugam

Selvi

Mandal

2012

International Journal of Biological Macromolecules

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Non-native States of Bovine Beta-Lactoglobulin Induced by Acetonitrile: pH-Dependent Unfolding of the Two Genetic Variants A and B

Naqvi

Ahmad

Khan

et al. 2012

Cell Biochem Biophys

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Acetonitrile (ACN)-induced unfolding of the beta-lactoglobulin variants A and B was investigated at pH 2.0, 7.0 and 9.0. ACN caused α-helix induction at low concentrations but lead to major conformational alterations when the concentration was raised. ACN also induced a concentration-dependent increase in the surface hydrophobicity of both the variants. Induction of α-helical structure and exposure of hydrophobic patches were, however, somewhat more pronounced in case of variant B, whereas the loss of tertiary structure was more marked for variant A. Both protein aggregation and helix induction necessitated higher ACN concentrations at pH 2.0 than at 7.0 and 9.0, suggesting the greater stability of the variants at acidic pH.

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Extraction, characterization of the polysaccharide extracts from Se-enriched G. lucidum (Se-GLP) and its inhibition against oxidative damage in ischemic reperfusion mice

Shi

Han

Chen

et al. 2010

Carbohydrate Polymers

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Acetonitrile-induced unfolding of porcine pepsin A

Cited by 10 publications

References 59 publications

Ethanol and acetonitrile induces conformational changes in porcine pepsin at alkaline denatured state

Ethanol and acetonitrile induces conformational changes in porcine pepsin at alkaline denatured state

Non-native States of Bovine Beta-Lactoglobulin Induced by Acetonitrile: pH-Dependent Unfolding of the Two Genetic Variants A and B

Extraction, characterization of the polysaccharide extracts from Se-enriched G. lucidum (Se-GLP) and its inhibition against oxidative damage in ischemic reperfusion mice

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