A protease-activatable collagen targeting probe (proCNA35) is synthesized by conjugation of a synthetic collagen fragment to the collagen binding protein CNA35via a protease-cleavable linker. Cleavage of the linker by MMP1 releases the intramolecular inhibition of the collagen binding site and restores its collagen binding capacity.
一种可被
蛋白酶激活的胶原靶向探针(proCNA35)是通过将合成的胶原片段与胶原结合蛋白CNA35通过一种可被
蛋白酶切割的连接子结合而合成的。MMP1切割该连接子后,释放了胶原结合位点的分子内抑制,并恢复其胶原结合能力。