Abstract
The cowpea chlorotic mottle virus (CCMV) is a nanoparticle that holds promise for diagnostic and therapeutic applications. The empty virus-like particle, however, is not stable under physiological conditions. Here, we describe a systematic study into the expansion of the assembly properties of a protein-based block copolymer of the CCMV capsid protein and an elastin-like polypeptide. By systematically changing the hydrophobicity of the stimulus-responsive elastin-like polypeptide block, assembly of the capsid proteins could be achieved at close to physiological conditions. This strategy may prove to be useful in the development of a physiologically stable CCMV capsid variant.
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