Analysis of Interaction between Dendriplexes and Bovine Serum Albumin

Shcharbin, Dzmitry; Pedziwiatr, Elzbieta; Chonco, Louis; Jf, Bermejo-Martín; Ortega, Paula; Mata, F. Javier de la; Eritja, Ramón; Gómez, Rafael; Klajnert, Barbara; Bryszewska, Maria; Ma, Muñoz-Fernández

doi:10.1021/bm070333p

Cited by 48 publications

(35 citation statements)

References 20 publications

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“…The rest of the dendriplexes formed by dendrimers 1, 2 and 4 afforded analogous results and a more detailed physicochemical study will be published separately. 18 The increase of the fluorescence polarization of fluorescein in the presence of dendrimers (Fig. 6A) or in the presence of BSA (Fig.…”

Section: Resultsmentioning

confidence: 94%

Water-soluble carbosilane dendrimers protect phosphorothioate oligonucleotides from binding to serum proteins

et al. 2007

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Treatment of dendriplexes formed between water-soluble carbosilane dendrimers and phosphorothioate oligodeoxynucleotides (ODN) with the anionic detergent sodium dodecyl sulfate disrupted the complexes indicating that the nature of the union in such dendriplexes is merely electrostatic. However, dendriplexes were not dissociated by serum proteins like bovine or human serum albumins, as assessed by gel electrophoresis and fluorescence experiments. This would imply a dendrimer-mediated protective effect able to prevent ODN interactions with serum proteins and additionally could translate into a reduction of the ODN doses needed to achieve the biological effects. The employment of carbosilane dendrimers as carriers may solve the problem of ODN kidnapping by plasmatic proteins as a key drawback for therapeutics involving ODNs. As examples, transfection processes on normal primary peripheral blood cells and diagnosis of HIV infection in the presence of serum have been assayed.

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Section: Resultsmentioning

confidence: 94%

Water-soluble carbosilane dendrimers protect phosphorothioate oligonucleotides from binding to serum proteins

et al. 2007

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“…This observation can be explained based on the existence of a special process in which the surfactant-cobalt(III) complex quenches BSA/HSA via initiation of a static mechanism rather than the dynamic process. 31,32 Similarly the binding number per albumin molecule (n) is around 1, indicating a strong and independent binding site in BSA/HSA for the surfactant-cobalt(III) complex. It is also observed that the binding (K b ) between the protein and the Table 2 The Stern-Volmer quenching constant (K sv ), quenching rate constant (k q ), binding constant (K b ), binding number (n) and the thermodynamic parameters (ΔH°, ΔG°and ΔS°) for the interaction of surfactant-cobalt(III) complexes with BSA/HAS at different temperatures Thermodynamic parameters and nature of the binding forces…”

Section: Analysis Of Quenching and Binding Parametersmentioning

confidence: 99%

Study of single and double chain surfactant–cobalt(iii) complexes and their hydrophobicity, micelle formation, interaction with serum albumins and antibacterial activities

Veeralakshmi

Nehru

Arunachalam

et al. 2014

Inorg. Chem. Front.

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To develop surfactant based metallodrugs, it is important to know the role of the tail part of the surfactant-metal complexes in their hydrophobicity, micellization behaviour, interaction with biomacromolecules and cell penetration. Here, we have taken a new series of single and double chain surfactant-cobalt(III) complexes with alkylamine ligands of different chain length, [Co(dien)(DA)Cl 2 ]ClO 4 (1), [Co(dien)(HA)-Cl 2 ]ClO 4 (2), [Co(dien)(DA) 2 Cl](ClO 4 ) 2 (3) and [Co(dien)(HA) 2 Cl](ClO4) 2 (4), where dien = diethylenetriamine, DA = dodecylamine and HA = hexadecylamine. The complexes were characterised by elemental analysis, NMR, ESI-MS, UV-visible and FTIR techniques. In addition, the average size distribution and morphology of self-assembled surfactant-cobalt(III) complexes were examined by DLS and SEM, respectively.The hydrophobicity, critical micelle concentration (CMC) values, thermodynamics of micellization (ΔG°m, ΔH°m and ΔS°m) and the nature of the interaction of these complexes with bovine and human serum albumins (BSA/HSA) were evaluated. The obtained CMC values were in the order 1 > 2 > 3 > 4, indicating that double chain systems have lower CMC values compared to single chain systems due to the increase in the hydrophobicity of the alkyl amine ligands. The thermodynamics of micellization indicated that the process is spontaneous, exothermic and entropy driven. The interaction of complexes 1-4 with serum albumins indicated that the quenching process follows a static mechanism, and the extent of quenching and binding parameters were in the order 1 < 2 < 3 < 4. Interestingly, on increasing the temperature, the protein-complex stability decreased for the single chain systems, and increased for the double chain systems, probably due to the involvement of electrostatic and hydrophobic interactions. This was further supported by the thermodynamics of protein interaction and synchronous fluorescence studies. Moreover, the results from UV-vis, synchronous and circular dichroism (CD) showed the occurrence of conformational and micro environmental changes in BSA/HSA. It is also noted that BSA has more binding affinity with surfactant-metal complexes compared to HSA. Furthermore, the antimicrobial effects of these complexes were investigated by disk diffusion method; complex 4 has a better antimicrobial activity due to the ease of bacterial cell penetration due to its more hydrophobic nature.

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“…10 Even though the interaction of dendrimers with bovine serum albumin (BSA) has been reported, the effect of polymer complexation on protein stability and secondary structure is not yet known. 11,12 Serum albumins are the major soluble protein constituents of the circulatory system and have many physiological functions. 13 The most important property of this group of proteins is that they serve as transporters for a variety of compounds.…”

Section: Introductionmentioning

confidence: 99%

Complexes of Dendrimers with Bovine Serum Albumin

2010

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We report the complexation of bovine serum albumin (BSA) with several dendrimers of different compositions mPEG-PAMAM (G3), mPEG-PAMAM (G4), and PAMAM (G4) at physiological conditions using constant protein concentration and various dendrimer contents. FTIR, CD, and fluorescence spectroscopic methods were used to analyze polymer binding mode, the binding constant, and the effects of dendrimer complexation on BSA stability and conformation. Structural analysis showed that dendrimers bind BSA via hydrophilic and hydrophobic interactions with a number of bound polymers (n): 1.30 for mPEG-PAMAM-G3, 1.30 for mPEG-PAMAM-G4, and 1.0 for PAMAM-G4. The polymer-BSA binding constants were K(mPEG-G3) = 5.0 (+/-0.8) x 10(3) M(-1), K(mPEG-G4) = 1.0 (+/-0.3) x 10(4) M(-1), and K(PAMAM-G4) = 1.1 (+/-0.4) x 10(4) M(-1). Dendrimer binding altered BSA conformation with a major reduction of alpha-helix and an increase in random coil and turn structures, indicating a partial protein unfolding.

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Analysis of Interaction between Dendriplexes and Bovine Serum Albumin

Cited by 48 publications

References 20 publications

Water-soluble carbosilane dendrimers protect phosphorothioate oligonucleotides from binding to serum proteins

Water-soluble carbosilane dendrimers protect phosphorothioate oligonucleotides from binding to serum proteins

Study of single and double chain surfactant–cobalt(iii) complexes and their hydrophobicity, micelle formation, interaction with serum albumins and antibacterial activities

Complexes of Dendrimers with Bovine Serum Albumin

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