Complex formation of albumin with tricarbocyanine dyes containing phosphonate groups

Кузьмин, В. А.; Nekipelova, T. D.; Podrugina, T. A.; Golovina, G. V.; Kostyukov, Alexey A.; Temnov, Viktor V.; Doroshenko, Irina A.; Radchenko, Eugene V.; Palyulin, V. A.; Зефиров, Н. С.

doi:10.1039/c6pp00246c

Cited by 15 publications

(13 citation statements)

References 34 publications

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“…Although the encapsulation efficiency of both agents is high, it is possible that the higher loading efficiency of ICG than of Dox is a result of higher binding affinity of this agent to the crosslinked albumin system via both electrostatic and hydrophobic interactions. [44][45][46] In addition, the encapsulation efficiency of both agents decreased as a function of target agent loading, as expected, as the number of available binding sites on the albumin particle decreases with increased loading. Selection of BSA as the carrier led to higher DL% for both agents is compared to our previous work where we utilized poly(lactic acid)-b-poly(ethylene glycol) as the carrier.…”

Section: Nanoparticle Preparation and Agent Loadingsupporting

confidence: 75%

Dual Photothermal/Chemotherapy of Melanoma Cells with Albumin Nanoparticles Carrying Indocyanine Green and Doxorubicin Leads to Immunogenic Cell Death

Aghda

Torres-Hurtado

Abdulsahib

et al. 2021

Macromolecular Bioscience

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Recent focus on cancer immunotherapies has led to significant interest in the development of therapeutic strategies that can lead to immunogenic cell death (ICD), which can cause activation of an immune response against tumor cells and improve immunotherapy outcomes by enhancing the immunogenicity of the tumor microenvironment. In this work, a nanomedicine-mediated combination therapy is used to deliver the ICD inducers doxorubicin (Dox), a chemotherapeutic agent, and indocyanine green (ICG), a photothermal agent. These agents are loaded into nanoparticles (NPs) of bovine serum albumin (BSA) that are prepared through a desolvation process. The formulation of BSA NPs is optimized to achieve NPs of 102.6 nm in size and loadings of 8.55 % and 5.69 % (w/w) for ICG and Dox, respectively. The controlled release of these agents from the BSA NPs is confirmed. Upon laser irradiation for 2.5 min, NPs at a dose of 62.5 𝝁g mL −1 are able to increase the temperature of the cells by 7 °C and thereby inhibit the growth of B16F10 melanoma cells in vitro. Surface presentation of heat shock proteins and calreticulin from the cells after treatment confirmed the ability of the Dox/ICG loaded BSA NPs to induce ICD in the melanoma cells.

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Section: Nanoparticle Preparation and Agent Loadingsupporting

confidence: 75%

Dual Photothermal/Chemotherapy of Melanoma Cells with Albumin Nanoparticles Carrying Indocyanine Green and Doxorubicin Leads to Immunogenic Cell Death

Aghda

Torres-Hurtado

Abdulsahib

et al. 2021

Macromolecular Bioscience

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“…The intramolecular rotational motions of the flexible polymethine chain in TC dyes would lead to rapid nonradiative decay. 15a , 19a , 21 As a result, noncovalent interactions (e.g., hydrogen bonding, hydrophobic interaction, and electrostatic attraction) with proteins are very likely to stabilize TC dyes, thus restricting the nonradiative decay caused by rotation and twist and hence increasing the quantum yield of these TC dyes. 22 Therefore, we hypothesize that the slightly red-shifted monomer absorption peak ( Figure S14C ) is also due to noncovalent interactions between the dye monomer and protein.…”

Section: Results and Discussionmentioning

confidence: 99%

Protein Discrimination Using a Fluorescence-Based Sensor Array of Thiacarbocyanine-GUMBOS

et al. 2020

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Sensitive and selective detection of proteins from complex samples has gained substantial interest within the scientific community. Early and precise detection of key proteins plays an important role in potential clinical diagnosis, treatment of different diseases, and proteomic research. In the study reported here, six different compounds belonging to a group of uniform materials based on organic salts (GUMBOS) have been synthesized using three thiacarbocyanine (TC) dyes and employed as fluorescent sensors. Fluorescence properties of micro- and nanoaggregates of these TC-based GUMBOS formed in phosphate buffer solutions are studied in the absence and presence of seven proteins. Fluorescence response patterns of these TC-based GUMBOS were analyzed by linear discriminant analysis (LDA). The constructed LDA model allowed discrimination of these seven proteins at various concentrations with 100% accuracy. The sensing and discrimination abilities of these TC-based GUMBOS were further evaluated in mixtures of two major proteins, i.e., human serum albumin and hemoglobin. Fluorescence response patterns of these mixtures were analyzed by LDA. This model allowed discrimination of various mixtures with 100% accuracy. Moreover, spiked urine samples were prepared and the responses of these sensors were collected and analyzed by LDA. Remarkably, discrimination of these seven proteins was also achieved with 100% accuracy.

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“…For Py-LYQLENY conjugate ( 2 ), the binding constants K b were calculated according to Equation (3) proposed by Kuzmin et al [ 63 ]: θ = K b ·[HSA] / (1+ K b ·[HSA]) where [HSA] is the concentration of the albumin [ 61 ], θ = (I − I 0 )/(I ∞ − I 0 ) is the fraction of the pyrene probe bound with HSA, I 0 is fluorescence intensity without HSA, I ∞ is fluorescence intensity with [HSA] = 45 µM (reaching a plateau, Figure 6 b) and I is the fluorescence intensity for subsequent acrylamide (ACR) concentrations used as a fluorescence quencher.…”

Section: Resultsmentioning

confidence: 99%

Human Serum Albumin Binds Native Insulin and Aggregable Insulin Fragments and Inhibits Their Aggregation

et al. 2020

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The purpose of this study was to investigate whether Human Serum Albumin (HSA) can bind native human insulin and its A13–A19 and B12–B17 fragments, which are responsible for the aggregation of the whole hormone. To label the hormone and both hot spots, so that their binding positions within the HSA could be identified, 4-(1-pyrenyl)butyric acid was used as a fluorophore. Triazine coupling reagent was used to attach the 4-(1-pyrenyl)butyric acid to the N-terminus of the peptides. When attached to the peptides, the fluorophore showed extended fluorescence lifetimes in the excited state in the presence of HSA, compared to the samples in buffer solution. We also analyzed the interactions of unlabeled native insulin and its hot spots with HSA, using circular dichroism (CD), the microscale thermophoresis technique (MST), and three independent methods recommended for aggregating peptides. The CD spectra indicated increased amounts of the α-helical secondary structure in all analyzed samples after incubation. Moreover, for each of the two unlabeled hot spots, it was possible to determine the dissociation constant in the presence of HSA, as 14.4 µM (A13–A19) and 246 nM (B12–B17). Congo Red, Thioflavin T, and microscopy assays revealed significant differences between typical amyloids formed by the native hormone or its hot-spots and the secondary structures formed by the complexes of HSA with insulin and A13–A19 and B12–B17 fragments. All results show that the tested peptide-probe conjugates and their unlabeled analogues interact with HSA, which inhibits their aggregation.

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Complex formation of albumin with tricarbocyanine dyes containing phosphonate groups

Cited by 15 publications

References 34 publications

Dual Photothermal/Chemotherapy of Melanoma Cells with Albumin Nanoparticles Carrying Indocyanine Green and Doxorubicin Leads to Immunogenic Cell Death

Dual Photothermal/Chemotherapy of Melanoma Cells with Albumin Nanoparticles Carrying Indocyanine Green and Doxorubicin Leads to Immunogenic Cell Death

Protein Discrimination Using a Fluorescence-Based Sensor Array of Thiacarbocyanine-GUMBOS

Human Serum Albumin Binds Native Insulin and Aggregable Insulin Fragments and Inhibits Their Aggregation

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