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. Author manuscript; available in PMC: 2021 Dec 17.
Published in final edited form as: Nat Nanotechnol. 2021 Jun 17;16(9):1030–1038. doi: 10.1038/s41565-021-00928-x

Figure 1. Generation of LNPs to target the high-affinity conformation of integrin α4β7.

Figure 1

a. Illustration of the generation of LNPs using microfluidics. The ionizable lipid facilitates siRNA encapsulation through its positive charge at low pH. b. Overview of the different domains of the MAdCAM-1-Fc fusion protein. c. Overview of the fusion strategy. The different domains of the wild type MAdCAM-1 are shown. Only the integrin binding domains D1 and D2 are used. D1D2 is fused to the hinge of rat IgG2a with a flexible linker. d. Schematic drawing depicting the conjugation strategy of the MAdCAM-1-Fc to the LNPs. The RG7 linker (mAb against rat IgG2a) is chemically conjugated with the LNPs to the maleimide group in the lipid DSPE-PEG-Maleimide. RG7 readily binds the MAdCAM-1-Fc by antibody affinity. e. LNP targeting to HA α4β7 integrin. CCL25 induces the integrin conformational change.