Yongping DongGang ChenYing ZhouJun‐Jie Zhu
Caspase-3 is one of the most frequently activated cysteine proteases during the apoptosis process and has been identified as a well-established cellular marker of apoptosis. In this study, a novel approach for the sensitive determination of caspase-3 activity was proposed using electrochemiluminescence (ECL) of Ru(bpy)3(2+)-doped silica (Ru@SiO2) with tripropylamine (TPA) as coreactant. A nanocomposite containing gold nanoparticles (AuNPs), poly(dimethyldiallyl ammonium chloride) (PDDA), and multiwalled carbon nanotubes (CNTs) was fabricated as an ECL platform. The biotinylated DEVD-peptide (biotin-Gly-Asp-Gly-Asp-Glu-Val-Asp-Gly-Cys) was immobilized on the nanocomposite surface via the strong bonding interaction between AuNPs and the thiol group. Then the streptavidin-modified Ru(bpy)3(2+)-doped silica (Ru@SiO2-SA) was immobilized on the ECL platform via the specific interaction between biotin and streptavidin to generate ECL signal. Caspase-3 can specifically recognize and cleave the N-terminus of DEVD, leading to the loss of the biotin label and the decrease of ECL intensity to determine the activity of caspase-3. The results revealed a new ECL avenue for the sensitive and specific monitor of caspase-3, and the platform could be utilized to evaluate anticancer drugs.
Liyan ZhengYuwu ChiQingqing ShuYongqiang DongLan ZhangGuonan Chen
V.M. Gol'dbergMichael KaplanLeonard J. SoltzbergJoseph GenevichRebecca BerryAlma BukhariSherina ChanMegan DamourLeigh M. FrigugliettiE. L. GunnKaren HoAshley JohnsonYin Yin LinAlisabet LowenthalSeiyam SuthRegina ToRegina YopakJason D. SlinkerGeorge G. MalliarasSamuel Flores-TorresHéctor D. Abruña
Annabell G. BonnOleksandr YushchenkoEric VautheyOliver S. Wenger