Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.22.32 (bromelain)
 1,025 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Dense extracellular matrix (ECM) severely impedes the spread of drugs in solid tumors and induces hypoxia, reducing chemotherapy efficiency. Different proteolytic enzymes, such as collagenase (Col) or bromelain, can directly attach to the surface of nanoparticles and improve their diffusion, but the method of ligation may also impair the enzymatic activity due to conformational changes or blockage of the active site. Herein, a "nanoenzyme capsule" was constructed by combining collagenase nanocapsules (Col-nc) with heavy-chain ferritin (HFn) nanocages encapsulating the chemotherapy drug doxorubicin (DOX) to enhance tumor penetration of the nanoparticles by hydrolyzing collagen from the ECM. Col-nc could protect the activity of the enzyme before reaching the site of action while being degraded under mildly acidic conditions in tumors, and the released proteolytic enzyme could digest collagen. In addition, HFn as a carrier could effectively load DOX and had a self-targeting ability, enabling the nanoparticles to internalize into cancer cells more effectively. From in vivo and in vitro studies, we found that collagen was effectively degraded by Col-nc/HFn(DOX) to increase the accumulation and penetration of nanoparticles in the solid tumor site and could alleviate hypoxia inside the tumor to enhance the antitumor effects of DOX. Therefore, the strategy of increasing nanoparticle penetration in this system is expected to provide a potential approach for the clinical treatment of solid tumors.
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PMID:Mild Acid-Responsive "Nanoenzyme Capsule" Remodeling of the Tumor Microenvironment to Increase Tumor Penetration. 3224 84

Antioxidant peptides are increasingly being recognized as food additives due to their effects on body human, regulating in vivo oxidative stress against oxidation of lipids and proteins. Meat by-products are rich sources of protein that can be employed for this purpose. Specifically, porcine liver can be used to prepare hydrolysates with antioxidant activity employing proteolytic enzymes such as alcalase, bromelain, papain and flavourzyme. In this study, the antioxidant activity of these four porcine liver hydrolysates was evaluated by 2,2-diphenyl-1-picrylhydrazyl (DPPH), ((2,2-azinobis-(3-ethyl-benzothiazoline-6-sulphonate) (ABTS), Ferric reducing antioxidant power assay (FRAP) and Oxygen radical absorbance capacity assay (ORAC) assays and the identification of bioactive peptides was carried out by SWATH-MS technology. According to the SDS-PAGE pattern, the proteolysis index and the free amino acids amount, the protein degradation was clearly different among the studied enzymes. Indeed, alcalase enzyme produced the release of small peptides, meanwhile flavourzyme produced higher level of free amino acids. The heatmap analysis showed a peptidomic pattern more differentiated for alcalase than for the other enzymes. The peptides most abundant and correlated with antioxidant capacity were APAAIGPYSQAVLVDR from uncharacterized protein, GLNQALVDLHALGSAR, ALFQDVQKPSQDEWGK and LSGPQAGLGEYLFER from ferritin and LGEHNIDVLEGNEQFINAAK from trypsinogen. The production and characterization of biopeptides is a new merging challenge of meat industry.
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PMID:Antioxidant activity and peptidomic analysis of porcine liver hydrolysates using alcalase, bromelain, flavourzyme and papain enzymes. 3323 91