Thursday, 18 January 2018

Smileband health topics


Cell-derived nanoparticles have been garnering increased attention due to their ability to mimic many of the natural properties displayed by their source cells. This top-down engineering approach can be applied toward the development of novel therapeutic strategies owing to the unique interactions enabled through the retention of complex antigenic information. Herein, we report on the biological functionalization of polymeric nanoparticles with a layer of membrane coating derived from cancer cells. The resulting core–shell nanostructures, which carry the full array of cancer cell membrane antigens, offer a robust platform with applicability toward multiple modes of anticancer therapy. We demonstrate that by coupling the particles with an immunological adjuvant, the resulting formulation can be used to promote a tumor-specific immune response for use in vaccine applications. Moreover, we show that by taking advantage of the inherent homotypic binding phenomenon frequently observed among tumor cells the membrane functionalization allows for a unique cancer targeting strategy that can be utilized for drug delivery applications.
Keywords: Nanomedicine, biomimetic nanoparticle, cellular membrane, cancer immunotherapy, targeted drug delivery, homotypic targeting.   The anti-cancer drug binds to cancerous cells' membrane protein, known as dehydroorotate dehydrogenase (DHODH).
The researchers analysed how fats, which are the building blocks of cell membranes, and drugs bind to DHODH. 
Study author Dr Erik Marklund, from Uppsala University, said: 'Our simulations show the enzyme uses a few lipids as anchors in the membrane.
'When binding to these lipids, a small part of the enzyme folds into an adapter that allows the enzyme to lift its natural substrate [the substance an enzyme acts on] out of the membrane.
'It seems the drug, since it binds in the same place, takes advantage of the same mechanism.'  
Potential for more selective treatments 
Study author Sir David Lane, from the Karolinska Institute, in Sweden, added: 'The study helps to explain why some drugs bind differently to isolated proteins and proteins that are inside cells.
'By studying the native structures and mechanisms for cancer targets, it may become possible to exploit their most distinct features to design new, more selective therapeutics

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