Abstract
Protein-surfactant interactions have been explored for decades owing to their widespread application in the pharmaceutical, food, and cosmetics industries and their importance to biochemical systems. However, they require further study owing to their compositional complexity and the innate limitations of current analytical approaches. In this review, we briefly introduce a series of individual approaches used for the qualitative and quantitative investigation of protein-surfactant interactions, including absorbance- or emission-based spectroscopy, scattering-based spectroscopy, mass spectrometry, calorimetry, computation and microscopy. More importantly, we then compare and evaluate various combinations of these approaches and provide comprehensive critical assessments and comments regarding their application to the advanced study of protein-surfactant interactions at the molecular level.
| Original language | English |
|---|---|
| Journal | Analytica Chimica Acta |
| DOIs | |
| Publication status | Published - 2019 Jan 1 |
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Keywords
- Calorimetry
- Combinations of analytical approaches
- Computation
- Microscopy
- Protein-surfactant interactions
- Spectroscopy and spectrometry
ASJC Scopus subject areas
- Analytical Chemistry
- Biochemistry
- Environmental Chemistry
- Spectroscopy
Cite this
Staring at protein-surfactant interactions : Fundamental approaches and comparative evaluation of their combinations - A review. / Li, Yan; Lee, Jae-Seung.
In: Analytica Chimica Acta, 01.01.2019.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - Staring at protein-surfactant interactions
T2 - Fundamental approaches and comparative evaluation of their combinations - A review
AU - Li, Yan
AU - Lee, Jae-Seung
PY - 2019/1/1
Y1 - 2019/1/1
N2 - Protein-surfactant interactions have been explored for decades owing to their widespread application in the pharmaceutical, food, and cosmetics industries and their importance to biochemical systems. However, they require further study owing to their compositional complexity and the innate limitations of current analytical approaches. In this review, we briefly introduce a series of individual approaches used for the qualitative and quantitative investigation of protein-surfactant interactions, including absorbance- or emission-based spectroscopy, scattering-based spectroscopy, mass spectrometry, calorimetry, computation and microscopy. More importantly, we then compare and evaluate various combinations of these approaches and provide comprehensive critical assessments and comments regarding their application to the advanced study of protein-surfactant interactions at the molecular level.
AB - Protein-surfactant interactions have been explored for decades owing to their widespread application in the pharmaceutical, food, and cosmetics industries and their importance to biochemical systems. However, they require further study owing to their compositional complexity and the innate limitations of current analytical approaches. In this review, we briefly introduce a series of individual approaches used for the qualitative and quantitative investigation of protein-surfactant interactions, including absorbance- or emission-based spectroscopy, scattering-based spectroscopy, mass spectrometry, calorimetry, computation and microscopy. More importantly, we then compare and evaluate various combinations of these approaches and provide comprehensive critical assessments and comments regarding their application to the advanced study of protein-surfactant interactions at the molecular level.
KW - Calorimetry
KW - Combinations of analytical approaches
KW - Computation
KW - Microscopy
KW - Protein-surfactant interactions
KW - Spectroscopy and spectrometry
UR - http://www.scopus.com/inward/record.url?scp=85062077986&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85062077986&partnerID=8YFLogxK
U2 - 10.1016/j.aca.2019.02.024
DO - 10.1016/j.aca.2019.02.024
M3 - Review article
C2 - 30967183
AN - SCOPUS:85062077986
JO - Analytica Chimica Acta
JF - Analytica Chimica Acta
SN - 0003-2670
ER -