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Experimental and Molecular Docking Studies on Enzyme-Driven Biohybrid-Inspired Micromotors Based on Amylose-b-(PEG-co-PBA) Inclusion Complexes.
Madadi, Mozhdeh; Khoee, Sepideh; Layegh, Hesam.
Afiliación
  • Madadi M; Polymer Laboratory, School of Chemistry, College of Science, University of Tehran, P.O. Box 141556455, Tehran 14155-6455, Iran.
  • Khoee S; Polymer Laboratory, School of Chemistry, College of Science, University of Tehran, P.O. Box 141556455, Tehran 14155-6455, Iran.
  • Layegh H; Polymer Laboratory, School of Chemistry, College of Science, University of Tehran, P.O. Box 141556455, Tehran 14155-6455, Iran.
Langmuir ; 40(10): 5214-5227, 2024 03 12.
Article en En | MEDLINE | ID: mdl-38469650
ABSTRACT
Amylose is a linear polysaccharide with a unique ability to form helical inclusion complexes with the appropriate guest components. Numerous studies have been conducted on encapsulation of bioactive compounds for various applications. In the biomedical field, biohybrid micro/nanomotors (MNMs) have emerged as innovative candidates due to their excellent biocompatible and biodegradable properties. This study was inspired by the biohybrid- and enzymatic-propelled MNMs and explored the potential of amylose inclusion complexes (ICs) in creating these MNMs. The study developed a new type of micromotor made from (PEG-co-PBA)-b-amylose. Nanoprecipitation, dimethyl sulfoxide (DMSO), and ultrasound-treated methods were employed to create spherical, thick crystalline, and rod-bacterial-like morphologies, respectively. Candida antarctica lipase B (CALB) was used as the catalytic fuel to induce the motion by the enzymatic degradation of ester linkages in the polymeric segment. Optical microscopy was utilized to observe the motion of the motors following incubation with enzyme concentrations of 5, 10, and 20% (w/w). The results demonstrated that the velocity of the motors increased proportionally with the percentage of added enzyme. Additionally, a comprehensive molecular docking evaluation with PyRx software provided insight into the interaction of the CALB enzyme with polymeric moieties and demonstrated a good affinity between the enzyme and polymer in the binding site. This study provides novel insight into the design and development of enzymatically driven polymeric micromotors and nanomotors.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Polímeros / Amilosa Idioma: En Revista: Langmuir Asunto de la revista: QUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Irán Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Polímeros / Amilosa Idioma: En Revista: Langmuir Asunto de la revista: QUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Irán Pais de publicación: Estados Unidos