Protein therapeutics is considered to be one of the most encouraging and decisive areas of recent times due to its specificity and low genetic risks compared to small molecule drugs. Although a wide array of brilliant vehicle designs has been reported, the key issues are still being the instability of protein in serum and lack of proper reversible protection throughout the delivery pathway. To address this issue, we have designed a robust biomolecular delivery vector that can be reversibly coupled with proteins and would effectively protect the payload until its intra-cellular delivery and consequent release. We envisaged the feasibility of exploiting a self-immolative backbone structure of a polymer to capture and release hydrophilic proteins tracelessly. The protein is conjugated through its surface exposed functional groups in aqueous media and protected by <i>shrink-wrapping</i> with crosslinking reaction. The activity of proteins was shown to be successfully turned off in the encapsulated state, and then switched on after releasing through redox stimuli. Efficacy of the polymeric cargo was evaluated with intracellular delivery of multiple protein payloads and reduction of cell viability for apoptotic proteins. In summary, the strategy reported herein provides a simple and robust delivery platform potentially applicable to a broad range of proteins and would help design the next generation therapeutics.

Shrink-wrapped encapsulation of proteins and triggered traceless release through reactive self-assembly approach

254th National Meeting (2017)

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