scholarly journals UJI TOKSISITAS DENGAN METODE BSLT PADA NANOPARTIKEL KOMBINASI OBAT CISPLATIN, BOVINE SERUM ALBUMIN DAN ASAM FOLAT

2021 ◽  
Vol 6 (1) ◽  
pp. 69-78
Author(s):  
Ersalina Nidianti ◽  
◽  
Ary Andini

Cancer is a non-communicable disease that causes morbidity and mortality in all regions of the world. Cancer treatment is important in reducing the high number of deaths (mortality) due to cancer sufferers. One of the cancer treatments is using chemotherapy drug cisplatin. However, cisplatin drug has side effects, namely nephrotoxicity, ototoxicity, neurotoxicity, hemotoxicity, cardiotoxicity, and hepatotoxicity. Therefore, the combination of cisplatin in albumin nanoparticles and modification of the bond using folic acid as an alternative solution minimizes the resulting toxic effects. This study aimed to determine the toxicity effect of the cisplatin drug formulation with a combination of bovine serum albumin (BSA) nanoparticles and folic acid through the Brine Shrimp Lethality Test (BSLT) method. The research methods used were BSA nanoparticle synthesis (NP-BSA), NP-BSA Synthesis with Cisplatin Drug (CP-NP-BSA), Folic Acid Synthesis with CP-NP-BSA Combination (As-CP-NP-BSA). Then, a toxicity test was carried out using the BSLT method to determine the toxicity level of BSA nanoparticles and the effect of adding folic acid in the cisplatin drug in the nanoparticles. The results showed that the absorbance of the 358 nm As-CP-NP-BSA UV-Vis spectrophotometer was 0.86. The toxicity level of the NP-BSA with the LC50 value was 69.23 ppm while the As-CP-NP-BSA LC50 toxicity level was 56.56 ppm. Nanoparticles consisting of a combination of bovine serum albumin, cisplatin and folic acid can be used as candidates for anticancer drugs

Nanomaterials ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 792
Author(s):  
Febri Baskoro ◽  
Selvaraj Rajesh Kumar ◽  
Shingjiang Jessie Lue

This study investigates the permeance and rejection efficiencies of different dyes (Rhodamine B and methyl orange), folic acid and a protein (bovine serum albumin) using graphene oxide composite membrane. The ultrathin separation layer of graphene oxide (thickness of 380 nm) was successfully deposited onto porous polyvinylidene fluoride-polyacrylic acid intermediate layer on nonwoven support layer using vacuum filtration. The graphene oxide addition in the composite membrane caused an increased hydrophilicity and negative surface charge than those of the membrane without graphene oxide. In the filtration process using a graphene oxide composite membrane, the permeance values of pure water, dyes, folic acid and bovine serum albumin molecules were more severely decreased (by two orders of magnitude) than those of the nonwoven/polyvinylidene fluoride-polyacrylic acid composite membrane. However, the rejection efficiency of the graphene oxide composite was significantly improved in cationic Rhodamine B (from 9% to 80.3%) and anionic methyl orange (from 28.3% to 86.6%) feed solutions. The folic acid and bovine serum albumin were nearly completely rejected from solutions using either nonwoven/polyvinylidene fluoride-polyacrylic acid or nonwoven/polyvinylidene fluoride-polyacrylic acid/graphene oxide composite membrane, but the latter possessed anti-fouling property against the protein molecules. The separation mechanism in nonwoven/polyvinylidene fluoride-polyacrylic acid membrane includes the Donnan exclusion effect (for smaller-than-pore-size solutes) and sieving mechanism (for larger solutes). The sieving mechanism governs the filtration behavior in the nonwoven/polyvinylidene fluoride-polyacrylic acid/graphene oxide composite membrane.


Author(s):  
John J. Turek ◽  
Christopher P. Leamon ◽  
Philip S. Low

Recently, methods for the delivery of macromolecules into cells via covalent coupling to vitamins have been described for plant and animal cells. This method utilizing vitamin receptor endocytosis concentrates macromolecules inside the cell in an active form that is nondegradative. The purpose of this study was to determine the specific location of bovine serum albumin-folic acid-colloidal gold (BSA-F-CG) conjugates within KB cells. Bovine serum albumin was covalently coupled to folic acid (BSA-F) and used to stabilize 15 nm colloidal gold (CG) particles. KB cells were incubated with BSA-F-CG or BSA-CG at either 11°C for 2 hours or 37°C for 15 minutes to allow binding, and the cells washed to remove unbound material. Some cells were fixed immediately, and others were incubated for additional time periods. BSA-CG particles nonspecifically pinocytosed by control cells were only found in large dense endosomes after 6 hours incubation. In cells incubated with BSA-F-CG, CG particles decorated the plasma membrane, and were found in uncoated pits. At 30 minutes CG particles could be found in multivesicular bodies (MVB’s), small vesicles, and dense endosomes. At 6 hours, CG particles were found in various dense endosomes, MVB’s, dense endosomes associated with the Golgi apparatus, and free in the cytoplasm. Cells that were pulsed with BSA-F-CG for 15 minutes at 37°C had CG particles on the surface and uncoated pits, small vesicles and MVB’s. After 60 and 360 minutes, BSA-F-CG was located in MVB’s, clear and dense endosomes, and MVB’s associated with the Golgi apparatus. Control cells incubated with BSA-CG had a few CG particles located in small clear endosomes at 15 minutes and large dense endosomes at 6 hours. For comparison, 5nm colloidal gold was stabilized with transferrin (TF) and incubated alone with KB cells or coincubated with 15 nm BSA-F-CG. The 5 nm TF-CG was localized in coated pits and on the rim of vesicular structures resembling CURL (Compartment of Uncoupling of Receptor and Ligand) at 15 minutes. There was no colocalization of TF-CG and BSA-F-CG at 15 minutes. TF-CG and BSA-F-CG were found separately and together in MVB’s at 1 hour. At six hours TF-CG and BSA-F-CG frequently colocalized in large dense endosomes. Folate labeled proteins endocytosed in this study shared some common compartments with transferrin, but there were several points of divergence. Transferrin-CG is taken up via coated pits whereas BSA-F-CG enters the cell via uncoated pits. At 15 minutes, internalized TF-CG is associated primarily with vesicles resembling CURL, and BSA-F-CG is found in MVB’s. At one hour, both TF-CG and BSA-F-CG may be found separately and together in MVB’s, and at 6 hours both may be found separately and together in dense endosomes. The BSA-F-CG particles free in the cytoplasm may be released during transport of the ligand, possibly by MVB’s that associate with the Golgi apparatus. The BSA-F-CG particles localized in this study may represent the normal location of endocytosed folate or their location could be an aberration of the normal pathway.


1993 ◽  
Vol 106 (1) ◽  
pp. 423-430 ◽  
Author(s):  
J.J. Turek ◽  
C.P. Leamon ◽  
P.S. Low

It has been demonstrated that proteins covalently conjugated to folic acid may be taken up by cells via endocytosis after binding to a folate binding protein (FBP) in the cell membrane. The proteins taken up in this manner remain catalytically active and they may modify physiological processes occurring in the cytosol. Confocal fluorescence microscopy of KB cells incubated with FITC-bovine serum albumin-folic acid conjugates showed that after uptake, the conjugates resided in large vesicular structures. The purpose of the present study was to determine the subcellular localization of protein-folic acid conjugates in KB cells using folic acid-bovine serum albumin-colloidal gold (F-BSA-CG) as a tracer. F-BSA-CG conjugates were taken up via uncoated pits or caveolae, and resided primarily in multivesicular bodies (MVBs) and other tubular endosomes at early time points (15-60 min). At later time points (6 hours), conjugates were still contained in MVBs but some were also found in secondary lysosomes or free in the cytoplasm. Coincubation of KB cells with transferrin-colloidal gold (TF-CG) and F-BSA-CG resulted in colocalization of TF-CG and F-BSA-CG within endosomal elements at times later than 15 minutes, indicating that the caveolae-mediated F-BSA-CG endocytic pathway converged with a pathway utilized by clathrin-coated pits.


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