DNA–Lysozyme Nanoarchitectonics: Quantitative Investigation on Charge Inversion and Compaction

Zhang, Rongyan; Wang, Yanwei; Yang, Guangcan

doi:10.3390/polym14071377

Cited by 10 publications

(8 citation statements)

References 39 publications

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“…Owing to the globules’ compact size compared to DNA molecules, they can easily bind to DNA strands in a “beads on a string” manner. Such binding can lead to the collapse of DNA strands with the formation of compact complexes at certain protein concentrations [ 17 ]. At the same time, the AFM data of this study show long DNA threads at the liquid surface ( Figure 3 b).…”

Section: Discussionmentioning

confidence: 99%

“…It is also a basic protein with an isoelectric point at about pH 11 [ 13 ], making it a suitable model for the investigation of DNA–protein interactions at the solution–air interface. It is well-established that DNA–lysozyme complex formation is driven predominantly by electrostatic interactions [ 14 , 15 , 16 , 17 , 18 ]. The morphology of DNA–lysozyme aggregates depends strongly on the molar ratio between the components.…”

Section: Introductionmentioning

confidence: 99%

“…Lundberg et al observed the formation of DNA/lysozyme flexible worm-like assemblies at low lysozyme to DNA molar ratios [ 18 ]. Zhang et al have recently demonstrated that the binding of lysozyme globules to DNA can result in the formation of both “over-” and “undercharged” complexes with a different morphology due to electrostatic interactions governed by the protein concentration [ 17 ]. Very recently, Morimoto et al studied the influence of high lysozyme concentrations under macromolecular crowding conditions, in [ 19 ].…”

Section: Introductionmentioning

confidence: 99%

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DNA Penetration into a Lysozyme Layer at the Surface of Aqueous Solutions

Chirkov

Lin²,

Michailov³

et al. 2022

IJMS

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The interactions of DNA with lysozyme in the surface layer were studied by performing infrared reflection–absorption spectroscopy (IRRAS), ellipsometry, surface tensiometry, surface dilational rheology, and atomic force microscopy (AFM). A concentrated DNA solution was injected into an aqueous subphase underneath a spread lysozyme layer. While the optical properties of the surface layer changed fast after DNA injection, the dynamic dilational surface elasticity almost did not change, thereby indicating no continuous network formation of DNA/lysozyme complexes, unlike the case of DNA interactions with a monolayer of a cationic synthetic polyelectrolyte. A relatively fast increase in optical signals after a DNA injection under a lysozyme layer indicates that DNA penetration is controlled by diffusion. At low surface pressures, the AFM images show the formation of long strands in the surface layer. Increased surface compression does not lead to the formation of a network of DNA/lysozyme aggregates as in the case of a mixed layer of DNA and synthetic polyelectrolytes, but to the appearance of some folds and ridges in the layer. The formation of more disordered aggregates is presumably a consequence of weaker interactions of lysozyme with duplex DNA and the stabilization, at the same time, of loops of unpaired nucleotides at high local lysozyme concentrations in the surface layer.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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DNA Penetration into a Lysozyme Layer at the Surface of Aqueous Solutions

Chirkov

Lin²,

Michailov³

et al. 2022

IJMS

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“…DNA-coated zein particles have been used for the encapsulation and protection of kaempferol or α-tocopherol [ 8 ]. Lysozyme-induced charge neutralization of DNA led to the formation of compact particles in a globule shape [ 9 ]. It is thus possible to develop the potential carriers for the delivery of BCs using lysozyme and DNA complex particles.…”

Section: Introductionmentioning

confidence: 99%

Encapsulation of Folic Acid and α-Tocopherol in Lysozyme Particles and Their Bioaccessibility in the Presence of DNA

Gao²,

Cheng

et al. 2023

Antioxidants

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Protein particles have been reported as the potential carriers for the co-encapsulation of bioactive components. In this study, lysozyme, a basic protein, was used to simultaneously encapsulate folic acid and α-tocopherol at pH 4.0. The encapsulation efficiency and loading capacity of folic acid or α-tocopherol increased with its respective concentration. Folic acid had no influence on the encapsulation of α-tocopherol. However, the encapsulation of folic acid was improved by α-tocopherol below 40 μg/mL but reduced by α-tocopherol at higher concentrations. The encapsulation by lysozyme shielded folic acid, α-tocopherol, or both partially from the attack of 2,2′-azino-bis-3-ethylbenzthiazoline-6-sulphonic acid (ABTS) radical cation. No masking effect of lysozyme encapsulation on α-tocopherol was found in DPPH antioxidant activity assay. Furthermore, the DNA coating was used to improve the dispersion of lysozyme with folic acid and α-tocopherol. The lysozyme/DNA particles with folic acid and α-tocopherol showed a homogenous size distribution of 180–220 nm with ζ-potential values between −33 and −36 mV. The release and bioaccessibility of folic acid in lysozyme/DNA with α-tocopherol were similar to that of folic acid alone, while the release of α-tocopherol was delayed and its bioaccessibility was improved by encapsulation in lysozyme/DNA with folic acid. The data gathered here would provide guidance for the use of lysozyme-based co-encapsulating carriers in the development of functional foods.

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“…Others use imaging such as atomic force microscopy, based on force spectroscopy (AFM-FS) [20,21], magnetic tweezers and dynamic light scattering [22,23]. Energy transfer such as Förster resonance energy transfer (FRET) [24,25], Bioluminescence resonance energy transfer (BRET) [26] and fluorescence cross-correlation spectroscopy (FCCS) [27,28] are also employed. In the case of serum-heme interactions, it is to be noted that the experimental difficulties are numerous, and the matrix is very complex.…”

Section: Introductionmentioning

confidence: 99%

Tracking Heme-Protein Interactions in Healthy and Pathological Human Serum in Native Conditions by Miniaturized FFF-Multidetection

et al. 2022

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The interaction of heme with blood serum proteins plays an important role in many physiological and pathological processes involving enzyme activity, gene expression and cell proliferation. The mechanisms underlying these interactions are; however, not yet fully understood. New analytical methods able to investigate protein-heme binding in native, biologically representative conditions are thus required. In this work, we present a method based on miniaturized, hollow-fiber flow field-flow fractionation with multiple spectrophotometric and light-scattering detection for size separation of high-abundance serum proteins and selective detection of heme-bound subpopulations. Heme is found to mainly interact with serum albumin, whereas a low amount also binds to other proteins such as IgM. The ability to bind heme in physiological conditions is also investigated for individual serum proteins. IgG is found unable to bind heme at clinically relevant concentrations. The proposed method allows separation, quantitation, and mass/size characterization of serum high-abundance proteins, providing information of heme-protein complex stability and preferred heme-clearing pathways. The same approach could be in perspective extended to the investigation of specific heme-antibody binding, and to further studies involving other molecules of pharmaceutical/clinical interest.

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DNA–Lysozyme Nanoarchitectonics: Quantitative Investigation on Charge Inversion and Compaction

Cited by 10 publications

References 39 publications

DNA Penetration into a Lysozyme Layer at the Surface of Aqueous Solutions

DNA Penetration into a Lysozyme Layer at the Surface of Aqueous Solutions

Encapsulation of Folic Acid and α-Tocopherol in Lysozyme Particles and Their Bioaccessibility in the Presence of DNA

Tracking Heme-Protein Interactions in Healthy and Pathological Human Serum in Native Conditions by Miniaturized FFF-Multidetection

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