A Review of Properties, Delivery Systems and Analytical Methods for the Characterization of Monomeric Glycoprotein Transferrin

Fernandes, Mariza Aires; Hanck-Silva, Gilmar; Baveloni, Franciele Garcia; Oshiro, João Augusto; Lima, Felipe Tita de; Eloy, Josimar O.; Chorilli, Marlus

doi:10.1080/10408347.2020.1743639

Cited by 8 publications

(8 citation statements)

References 84 publications

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“…Transferrin is a serum protein responsible for iron transport (reviewed in [60]). Transferrin has two Fe 3+ binding sites with dissociation constants of the order of 10 −22 M. At the same time, transferrin does not bind ferro-iron.…”

Section: Iron Binding Proteinsmentioning

confidence: 99%

“…Free iron ions induce formation of free radicals, which cause oxidative damages of tissues. Transferrins are a group of iron-binding proteins that control the levels of iron in the body fluids of vertebrates due to their ability to bind two Fe 3+ and two CO 3 2− (reviewed in [60]). The primary role of transferrin is therefore to transport iron safely around the body to supply growing cells.…”

Section: Iron Binding Proteinsmentioning

confidence: 99%

“…19 intra-chain disulfide bonds stabilize the transferrin molecule. Transferrin possesses three carbohydrate side chains attached to nitrogen of Asn413 and Asn611 and to oxygen of Ser32 (reviewed in [60,71]). The transferrin molecule consists of the N-lobe (336 amino acids) and C-lobe (343 amino acids), which are linked by a short spacer sequence.…”

Section: Iron Binding Proteinsmentioning

confidence: 99%

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Metal Binding Proteins

Permyakov

2021

Encyclopedia

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Metal ions play several major roles in proteins: structural, regulatory, and enzymatic. The binding of some metal ions increase stability of proteins or protein domains. Some metal ions can regulate various cell processes being first, second, or third messengers. Some metal ions, especially transition metal ions, take part in catalysis in many enzymes. From ten to twelve metals are vitally important for activity of living organisms: sodium, potassium, magnesium, calcium, manganese, iron, cobalt, zinc, nickel, vanadium, molybdenum, and tungsten. This short review is devoted to structural, physical, chemical, and physiological properties of proteins, which specifically bind these metal cations.

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Section: Iron Binding Proteinsmentioning

confidence: 99%

Section: Iron Binding Proteinsmentioning

confidence: 99%

Section: Iron Binding Proteinsmentioning

confidence: 99%

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Metal Binding Proteins

Permyakov

2021

Encyclopedia

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“…Lakkadawala et al [ 25 ] proposed the development of two liposomes containing cell-penetrating peptide (TAT or QLPVM peptides) and transferrin (Tf) for codelivery of doxorubicin and erlotinib (Tf-TAT-LIP and Tf-QLPVM-LIP, respectively) to treat GBM. Transferrin (Tf) is a serum glycoprotein that has been widely used to functionalize nanosystems to improve their transport across BBB and promote increased drug uptake by GBM cells through specific receptors overexpressed in cellular membranes [ 26 ]. Both liposomes were produced by thin-film hydration method and presented a mean size of 174.90 ± 4.45 nm and 175.57 ±, polydispersity index (PDI) of 0.254 ± 0.03 and 0.246 ± 0.02 and zeta potential of 15.03 ± 3.94 mV and 14.87 ± 0.53 mV for Tf-TAT-LIP and Tf-QLPVM-LIP, respectively.…”

Section: Lipid-based Drug Delivery Nanosystemsmentioning

confidence: 99%

Drug Delivery Nanosystems in Glioblastoma Multiforme Treatment: Current State of the Art

Filippo

Duarte

Luiz

et al. 2021

Self Cite

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: Glioblastoma multiforme (GBM) is the most common primary malignant Central Nervous System cancer, responsible for about 4% of all deaths associated with neoplasia, characterized as one of the most fatal human cancers. Tumor resection does not possess curative character, thereby radio and/or chemotherapy are often necessary for the treatment of GBM. However, drugs used in GBM chemotherapy present some limitations, such as side effects associated with nonspecific drug biodistribution as well as limited bioavailability, which limits their clinical use. To attenuate the systemic toxicity and overcome the poor bioavailability, a very attractive approach is drug encapsulation in drug delivery nanosystems. The main focus of this review is to explore the actual cancer global problem, enunciate barriers to overcome in the pharmacological treatment of GBM, as well as the most updated drug delivery nanosystems for GBM treatment and how they influence biopharmaceutical properties of anti-GBM drugs. The discussion will approach lipid-based and polymeric nanosystems, as well as inorganic nanoparticles, regarding their technical aspects as well as biological effects in GBM treatment. Furthermore, the current state of the art, challenges to overcome and future perspectives in GBM treatment will be discussed.

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“…Transferrin's mechanism of iron transport draws special attention because it occurs in endothelial cells of the blood-brain barrier. These tightly bound cells restrict the influx of material from the bloodstream, limiting the possibilities of treatment for various neurological diseases; however, transferrin is able to cross this barrier thanks to receptor-mediated endocytosis [5,6]. Moreover, transferrin is not limited to binding iron, and it may bind other molecules of therapeutic interest [7][8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

X-ray Characterization of Conformational Changes of Human Apo- and Holo-Transferrin

Campos-Escamilla

Siliqi

González-Ramírez

et al. 2021

IJMS

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Human serum transferrin (Tf) is a bilobed glycoprotein whose function is to transport iron through receptor-mediated endocytosis. The mechanism for iron release is pH-dependent and involves conformational changes in the protein, thus making it an attractive system for possible biomedical applications. In this contribution, two powerful X-ray techniques, namely Macromolecular X-ray Crystallography (MX) and Small Angle X-ray Scattering (SAXS), were used to study the conformational changes of iron-free (apo) and iron-loaded (holo) transferrin in crystal and solution states, respectively, at three different pH values of physiological relevance. A crystallographic model of glycosylated apo-Tf was obtained at 3.0 Å resolution, which did not resolve further despite many efforts to improve crystal quality. In the solution, apo-Tf remained mostly globular in all the pH conditions tested; however, the co-existence of closed, partially open, and open conformations was observed for holo-Tf, which showed a more elongated and flexible shape overall.

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A Review of Properties, Delivery Systems and Analytical Methods for the Characterization of Monomeric Glycoprotein Transferrin

Cited by 8 publications

References 84 publications

Metal Binding Proteins

Metal Binding Proteins

Drug Delivery Nanosystems in Glioblastoma Multiforme Treatment: Current State of the Art

X-ray Characterization of Conformational Changes of Human Apo- and Holo-Transferrin

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