ovalbumin and dodecyltrimethylammonium

ovalbumin has been researched along with dodecyltrimethylammonium* in 1 studies

Other Studies

1 other study(ies) available for ovalbumin and dodecyltrimethylammonium

Article	Year
Protein binding-induced surfactant aggregation variation: a new strategy of developing fluorescent aqueous sensor for proteins. ACS applied materials & interfaces, 2015, Mar-04, Volume: 7, Issue:8 Novel strategies of developing fluorescent sensors for proteins are highly demanded. In this work, we particularly synthesized a cholesterol-derivatized pyrene probe. Its fluorescence emission is effectively tuned by the aggregation state of a cationic surfactant dodecyltrimethylammonium bromide (DTAB). The used probe/DTAB assemblies exhibit highly sensitive ratiometric responses to pepsin and ovalbumin egg (o-egg) with detection limits of 4.8 and 18.9 nM, respectively. The fluorescence changes indicate the protein-surfactant interaction leads to further aggregation of DTAB assemblies. The results from Tyndall effect and dynamic light scattering verify this assumption. The responses to pepsin and o-egg are due to their strong electrostatic or hydrophobic interaction with DTAB assemblies at pH 7.4. The present noncovalent supramolecular sensor represents a novel and simple strategy for sensing proteins, which is based on the encapsulated fluorophore probing the aggregation variation of the surfactant assemblies. Topics: Cholesterol; Fluorescent Dyes; Micelles; Ovalbumin; Pepsin A; Protein Binding; Pyrenes; Quaternary Ammonium Compounds; Spectrometry, Fluorescence; Surface-Active Agents; Water	2015

Article

Year

Protein binding-induced surfactant aggregation variation: a new strategy of developing fluorescent aqueous sensor for proteins.

ACS applied materials & interfaces, 2015, Mar-04, Volume: 7, Issue:8

Novel strategies of developing fluorescent sensors for proteins are highly demanded. In this work, we particularly synthesized a cholesterol-derivatized pyrene probe. Its fluorescence emission is effectively tuned by the aggregation state of a cationic surfactant dodecyltrimethylammonium bromide (DTAB). The used probe/DTAB assemblies exhibit highly sensitive ratiometric responses to pepsin and ovalbumin egg (o-egg) with detection limits of 4.8 and 18.9 nM, respectively. The fluorescence changes indicate the protein-surfactant interaction leads to further aggregation of DTAB assemblies. The results from Tyndall effect and dynamic light scattering verify this assumption. The responses to pepsin and o-egg are due to their strong electrostatic or hydrophobic interaction with DTAB assemblies at pH 7.4. The present noncovalent supramolecular sensor represents a novel and simple strategy for sensing proteins, which is based on the encapsulated fluorophore probing the aggregation variation of the surfactant assemblies.

Topics: Cholesterol; Fluorescent Dyes; Micelles; Ovalbumin; Pepsin A; Protein Binding; Pyrenes; Quaternary Ammonium Compounds; Spectrometry, Fluorescence; Surface-Active Agents; Water

2015