We report a new route to synthesize clusters, or so-called colloidal molecules (CMs), which mimic the symmetry of molecular structures made of one central atom. We couple site-specifically functionalized patchy nanoparticles, i.e., valence-endowed colloidal atoms (CAs), with complementary nanospheres through amide bonds. By analogy with the Gillespie formalism, we show that AX, AXE and AXE CMs can be obtained from tetravalent sp-like CAs when the relative amount of both building units is varied in a controlled manner. We obtain AX CMs from divalent sp-like CAs. We also show that it is possible to covalently attach two different types of satellites to the same central patchy nanoparticle to create more complex CMs, opening the way to the fabrication of new multifunctional nanostructures with well-controlled shape and composition.
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http://dx.doi.org/10.3762/bjnano.9.278 | DOI Listing |
Fish Shellfish Immunol
June 2019
School of Marine Science, Ningbo University, Zhejiang, Ningbo, 315211, China; Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao, 266237, China. Electronic address:
Beilstein J Nanotechnol
December 2018
CNRS, Univ. Bordeaux, CRPP, UMR 5031, 115, av. du Dr Albert Schweitzer 33600 Pessac, France.
We report a new route to synthesize clusters, or so-called colloidal molecules (CMs), which mimic the symmetry of molecular structures made of one central atom. We couple site-specifically functionalized patchy nanoparticles, i.e.
View Article and Find Full Text PDFJ Virol
December 2014
Institute of Organic Chemistry and Biochemistry IOCB Research Centre and Gilead Sciences, Academy of Sciences of the Czech Republic, v.v.i., Flemingovo nam. 2, 166 10, Prague 6, Czech Republic Department of Biotechnology, Institute of Chemical Technology, Technická 5, Prague, Czech Republic
Unlabelled: The hexameric lattice of an immature retroviral particle consists of Gag polyprotein, which is the precursor of all viral structural proteins. Lentiviral and alpharetroviral Gag proteins contain a peptide sequence called the spacer peptide (SP), which is localized between the capsid (CA) and nucleocapsid (NC) domains. SP plays a critical role in intermolecular interactions during the assembly of immature particles of several retroviruses.
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