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The amount of the released MMP-1 mass was measured by the MMP-1 ELISA kit [17].
We found minimal difference in terms of the enzymatic activity between the encapsulated MMP-1 and free MMP-1 (0.03763 ± 0.0012 vs. 0.03879 ± 0.0008).
Despite the reductions in protease sensitivity, MMP-1 bound to all of the engineered rhCIIIs with comparable affinity, indicating that MMP-1 binding is not sufficient for cleavage.
Herein, we prepared novel MMP-1-loaded poly(lactide-co-glycolide-co-caprolactone) (PLGA-PCL) nanoparticles (NPs) capable of sustained release of MMP-1.
Taken together, we reported here novel PLGA-PCL NPs for sustained release of MMP-1, which may provide an ideal MMP-1 delivery approach for tissue reconstruction therapy.
Results were expressed as cumulative release of MMP-1 from NPs with three replicates.
Moreover, we characterized the optimized MMP-1-containing PLGA-PCL NPs by DLS and SEM.
Briefly, samples were centrifuged (20,000 × g at 4 °C for 10 min), and free MMP-1 in the supernatant was determined using the MMP-1 ELISA kit as per manufacturer's protocol: 100 μL of MMP-1 standard solution or MMP-1-containing samples were added into the microtiter plate wells, and then, all unbound sites were blocked to prevent false positive results.
The molecular descriptors most relevant to MMP-1 inhibitors were also derived from these 189 features.
In addition, hTERT expression resulted in the down-regulation of MMP-1.
Matrix metalloproteinase (MMP -1 degrades fibrillar collagens suggesting iMMP -1nt role in vascular remodegrades
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