Biomimetic assembly of polyelectrolyte multilayers containing phosvitin monitored with reflectometric interference spectroscopy

Grohmann, Steffi; Rothe, Holger; Eisenhuth, Susanne; Hoffmann, Christian; Liefeith, Klaus

doi:10.1116/1.3589176

Cited by 14 publications

(10 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Both effects almost compensate each other, such that the buildup is ineffective. Recently, Grohmann et al also reported cyclical evolution of the dry mass by means of an optical technique (reflectometric interference spectroscopy, RIfS), during the buildup of PhV/PLL films built up in close conditions, but the presence of a PEI precursor layer . At first sight, however, respective evolutions of the dry mass described by these authors and of the wet mass described here appear to be contradictory, as they varied in the opposite way for a given PLL or PhV injection.…”

Section: Resultsmentioning

confidence: 55%

“…Subsequent PhV adsorption step brings the QCM-D parameters back to values similar to those measured at the end of the preceding PhV adsorption step. This corresponds, in particular, to a wet mass uptake, whereas Grohmann et al detected a dry mass loss upon contact with the protein . PhV thus necessarily causes the desorption of the PLL molecules immobilized during the intermediate step and the uptake of water.…”

Section: Discussionmentioning

confidence: 98%

“…To our knowledge, very few studies have inspected the interactions of phosphoproteins with LbL films: Szyk-Warszyńska et al and Halthur et al described the effective buildup of films comprised of caseins and amelogenin, respectively, both in association with PLL, and only recently, Grohmann et al reported on the buildup of PhV/PLL films . Here, we attempted two immobilization modes of PhV into LbL films, (i) using PhV as the polyanionic component of PhV/PLL architectures and (ii) bringing preformed chondroitin sulfate (ChS)/PLL films in contact with PhV.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Protein-Triggered Instant Disassembly of Biomimetic Layer-by-Layer Films

et al. 2011

View full text Add to dashboard Cite

Layer-by-Layer (LbL) coatings are promising tools for the biofunctionalization of biomaterials, as they allow stress-free immobilization of proteins. Here, we explore the possibility to immobilize phosvitin, a highly phosphorylated protein viewed as a model of bone phosphoproteins and, as such, a potential promotive agent of surface-directed biomineralization, into biomimetic LbL architectures. Two immobilization protocols are attempted, first, using phosvitin as the polyanionic component of phosvitin/poly-(L-lysine) films and, second, adsorbing it onto preformed chondroitin sulfate/poly-(L-lysine) films. Surprisingly, it is neither possible to embed phosvitin as the constitutive polyanion of the LbL architectures nor to adsorb it atop preformed films. Instead, phosvitin triggers instant massive film disassembly. This unexpected, incidentally detected behavior constitutes the first example of destructive interactions between LbL films and a third polyelectrolyte, a fortiori a protein, which might open a route toward new stimuli-responsive films for biosensing or drug delivery applications. Interestingly, additional preliminary results still indicate a promotive effect of phosvitin-containing remnant films on calcium phosphate deposition.

show abstract

Section: Resultsmentioning

confidence: 55%

Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Protein-Triggered Instant Disassembly of Biomimetic Layer-by-Layer Films

et al. 2011

View full text Add to dashboard Cite

show abstract

“…Phosvitin is the most phosphorylated protein found in nature [ 11 , 12 ] and binds up to 127 calcium ions at pH 6.5 [ 12 ]. Accounting for 60% of chicken egg yolk phosphoproteins, this protein possesses redox activity [ 13 ], facilitates biomineralization [ 14 , 15 ], and acts as an antibiotic when bacteria are placed under stress [ 16 , 17 ]. In addition to undergoing calcium-induced conformational changes [ 18 – 20 ], phosvitin is thought to form calcium–phosvitin aggregates in the presence of high concentrations of calcium and has hydrophobic patches at its N − and C − termini [ 18 , 19 ].…”

Section: Introductionmentioning

confidence: 99%

Activity of Phosvitin in Hydroxyapatite Acid-Damage Immersion and Antimicrobial Assays

Shipman

Doering

Hemsath

et al. 2020

Biochemistry Research International

View full text Add to dashboard Cite

Phosvitin, the most highly phosphorylated metal-binding protein found in nature, binds more than 100 calcium ions, and has been identified as an agent that could be used to generate biomineralization scaffolds. Because of published reports describing phosvitin’s affinity for calcium and potential antibiotic activity, this study was undertaken in order to evaluate phosvitin for both antibiotic activity against common microorganisms and the ability to protect hydroxyapatite surfaces from acid damage. To more clearly define its antibiotic action, the effects of phosvitin on Micrococcus luteus, P. mirabilis, B. cereus, E. coli, and S. epidermidis were evaluated. In both Kirby–Bauer tests and liquid culture growth inhibition assays, phosvitin inhibited M. luteus, a microorganism that thrives in the human mouth, but not the other bacteria tested. The MIC of phosvitin was determined to be 31.3 μg/mL when delivered in 1 mM CaCl2 but was 0.5 mg/mL in the absence of added calcium. Expanding on the potential impacts of phosvitin on the mouth, its action was evaluated in a model of tooth decay represented by acid-damaged hydroxyapatite discs. SEM, AFM, and FAAS analyses revealed that pretreatment of discs with phosvitin modulated the damage-induced morphology and topography changes associated with acid-damaged discs.

show abstract

“…纳米生物界面调控着纳米材料的整体物理化学、药理和毒理学特性, 包括它们在血液中的快速清除、失去靶向能力, 激活免疫反应等 [21][22] [23][24][25] 、糖蛋白检测 [26] , 凝血酶抑制剂的高通量筛选 [27] , 细胞膜蛋白检测 [28] 和全细胞检测等研究 [29] . RIfS 实时原位检测生物过程是基于白光在基底层上下边界的反射导致反射干涉现象 [30] , 因此 RIfS 可以估计基底内部结合变化反应, 这意味可以用这种方法监测基底内部的蛋白冠引起的光学厚度的变化.…”

unclassified

A Novel Protein Corona Characterization based on the Reflectometric Interference Spectroscopy with Silica Colloidal Crystal Films

Wu¹,

Su²,

Zhou³

et al. 2021

Acta Chimica Sinica

View full text Add to dashboard Cite

It will form protein corona on the surface of nanoparticles when exposed to the biological environment. The process of protein corona formation is crucial in biomedical engineering, nanomaterials development and research, especially the protein corona formation process of medical engineering materials in blood samples, and there is no mature method for realtime monitoring. Silica colloidal crystal films were prepared by vertical deposition on the glass slides. The glass slides were placed vertically in an ethanol suspension of silica nonospheres with diameters of 110, 190 and 280 nm. After 7 days of ethanol evaporation, a large area of silica colloidal crystal film was formed on the surface of the glass slide. The glass slides of silica colloidal crystal films were assembled into reaction cell, and the reflectometric interference spectroscopy (RIfS) system assembled by microscope light source and spectrometer were used for detection and optical thickness as a parameter. And different concentrations of hydrochloric acid were used to test the performance of the RIfS system. In this study, RIfS was utilized to detect the protein corona formation of human serum albumin, human fibrinogen and immunoglobulin G, as well as blood samples by silica colloidal crystal films which have special optical properties. It was found that the formation of immunoglobulin G had the highest optical thickness variation due to its conformation. According to the formation process of human serum albumin on silica nanosheres with different diameters, the optical thickness of protein corona was also higher on the of silica nanospheres with higher curvature. In addition, through the detection of plasma and whole blood samples, it was found that the silica colloidal crystal films could basically eliminate the interference of blood cells to the detection of protein corona. This work developed a real-time unlabeled protein corona research method, which provides a basis for the clinical application of biomedical materials. Keywords plasma protein; protein corona; reflectometric interference spectroscopy; silica colloidal crystal film; ordered porous layer interferometry

show abstract

Biomimetic assembly of polyelectrolyte multilayers containing phosvitin monitored with reflectometric interference spectroscopy

Cited by 14 publications

References 29 publications

Protein-Triggered Instant Disassembly of Biomimetic Layer-by-Layer Films

Protein-Triggered Instant Disassembly of Biomimetic Layer-by-Layer Films

Activity of Phosvitin in Hydroxyapatite Acid-Damage Immersion and Antimicrobial Assays

A Novel Protein Corona Characterization based on the Reflectometric Interference Spectroscopy with Silica Colloidal Crystal Films

Contact Info

Product

Resources

About