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An Amylase-Responsive Bolaform Supra-Amphiphile.
Kang, Yuetong; Cai, Zhengguo; Tang, Xiaoyan; Liu, Kai; Wang, Guangtong; Zhang, Xi.
Afiliación
  • Kang Y; Key Lab of Organic Optoelectronics and Molecular Engineering, Department of Chemistry, Tsinghua University , Beijing 100084, P. R. China.
  • Cai Z; Key Lab of Organic Optoelectronics and Molecular Engineering, Department of Chemistry, Tsinghua University , Beijing 100084, P. R. China.
  • Tang X; Key Lab of Organic Optoelectronics and Molecular Engineering, Department of Chemistry, Tsinghua University , Beijing 100084, P. R. China.
  • Liu K; Key Lab of Organic Optoelectronics and Molecular Engineering, Department of Chemistry, Tsinghua University , Beijing 100084, P. R. China.
  • Wang G; Key Laboratory of Microsystems and Micronanostructures Manufacturing (Harbin Institute of Technology), Ministry of Education, Harbin 150080, P. R. China.
  • Zhang X; Key Lab of Organic Optoelectronics and Molecular Engineering, Department of Chemistry, Tsinghua University , Beijing 100084, P. R. China.
ACS Appl Mater Interfaces ; 8(7): 4927-33, 2016 Feb.
Article en En | MEDLINE | ID: mdl-26824642
An amylase-responsive bolaform supra-amphiphile was constructed by the complexation between ß-cyclodextrin and a bolaform covalent amphiphile on the basis of host-guest interaction. The bolaform covalent amphiphile could self-assemble in solution, forming sheet-like aggregates and displaying weak fluorescence because of aggregation-induced quenching. The addition of ß-cyclodextrin led to the formation of the bolaform supra-amphiphile, prohibiting the aggregation of the bolaform covalent amphiphile and accompanying with the significant recovery of fluorescence. Upon the addition of α-amylase, with the degradation ß-cyclodextrin, the fluorescence of the supra-amphiphile would quench gradually and significantly, and the quenching rate linearly correlated to the concentration of α-amylase. This study enriches the field of supra-amphiphiles on the basis of noncovalent interactions, and moreover, it may provide a facile way to estimate the activity of α-amylase.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Técnicas Biosensibles / Beta-Ciclodextrinas / Amilasas Idioma: En Revista: ACS Appl Mater Interfaces Asunto de la revista: BIOTECNOLOGIA / ENGENHARIA BIOMEDICA Año: 2016 Tipo del documento: Article

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Técnicas Biosensibles / Beta-Ciclodextrinas / Amilasas Idioma: En Revista: ACS Appl Mater Interfaces Asunto de la revista: BIOTECNOLOGIA / ENGENHARIA BIOMEDICA Año: 2016 Tipo del documento: Article
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