tailieunhanh - báo cáo khoa học: "Stability and assembly in vitro of bacteriophage PP7 virus-like particles"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Stability and assembly in vitro of bacteriophage PP7 virus-like particles | Journal of Nanobiotechnology BioMed Central Research Stability and assembly in vitro of bacteriophage PP7 virus-like particles Jerri C Caldeira and David S Peabody Open Access Address Department of Molecular Genetics and Microbiology University of New Mexico School of Medicine Albuquerque NM87131 USA Email Jerri C Caldeira-jcaldeira@ David S Peabody - dpeabody@ Corresponding author Published 26 November 2007 Received 29 June 2007 I. rr r Accepted 26 November 2007 Journal of Nanobiotechnology 2007 5 10 doi 186 1477-3155-5-10 This article is available from http content 5 1 10 2007 Caldeira and Peabody licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background The stability of a virus-like particle VLP is an important consideration for its use in nanobiotechnology. The icosahedral capsid of the RNA bacteriophage PP7 is cross-linked by disulfide bonds between coat protein dimers at its 5-fold and quasi-6-fold symmetry axes. This work determined the effects of these disulfides on the VLP s thermal stability. Results Measurements of the thermal denaturation behavior of PP7 VLPs in the presence and absence of a reducing agent show that disulfide cross-links substantially stabilize them against thermal denaturation. Although dimers in the capsid are linked to one another by disulfides the two subunits of dimers themselves are held together only by non-covalent interactions. In an effort to confer even greater stability a new cross-link was introduced by genetically fusing two coat protein monomers thus producing a single-chain dimer that assembles normally into a completely cross-linked VLP. However subunit fusion failed to increase the thermal stability of the .