Protein-adsorption behavior

Since Diaz and Balkus first attempted to immobilize enzymes on mesoporous MCM-41 [101], several research groups have investigated the influence of various physical factors such as pore size, ambient pH, and ionic strength, on the adsorption efficiency of proteins [102-118]. This research revealed the general tendencies of protein adsorption behavior and outlines for successful immobilization of proteins onto mesoporous materials. As one of the representative examples, systematic... 

As seen in the comparison of mesoporous silica and PMO in protein adsorption behavior, the nature of the framework of mesoporous materials has unavoidable influence on the protein adsorption. Therefore, adsorption of protein on mesoporous structures composed of hydrophobic materials such as carbon is worthy of detailed investigation. In this section, systematic research on protein adsorption on mesoporous carbon materials by Vinu and coworkers is mainly introduced. 

When cells are suspended in a biological fluid or culture medium, both serum proteins and cells interact with the surface substrate. Serum protein adsorption behavior on SAMs has been examined with various analytical methods, including SPR [58-61], ellipsometry [13, 62, 63], and quartz QCM [64—66]. These methods allow in situ, highly sensitive detection of protein adsorption without any fluorescence or radioisotope labeling. SPR and QCM are compatible with SAMs that comprise alkanethiols. In our laboratory, we employed SPR to monitor protein adsorption on SAMs. 

In Sect. 2, the author discusses protein adsorptive behavior of various polymeric materials in terms of their hydrophilicity or hydrophobicity. 

It is seen from Tables 3, 4, and 5 that almost all of the values of the global interaction parameters (gs) are negative (gs < 0). This is compatible with our knowledge concerning the protein-adsorption behavior of polymeric materials. 

Polymeric Materials with Ionic Functional Groups and Their Protein Adsorptive Behavior... 

The third example to be mentioned is the protein-adsorption behavior of PEUU samples which are coated or loaded with D1PAM or Methacrol, as discussed in Section 4.1. 

Hydrophilicity and hydrophobicity are the most fundamental properties to be controlled for materials whenever they are utilized in biomedical devices. Protein-adsorption behavior on several biomaterials of different hydrophilicity was discussed by comparing available data with two modellings (Ikada and Peppas) for the protein-adsorption process. The adsorptive behavior of poly(HEMA) carrying polyamine functional groups was also discussed. It is well-known that protein adsorption is the first event when any of the body fluids encounters an artificial material. 

The surface properties of the protein molecules, especially hydro-phobicity, as well as the degree of the sorbent surface hydropho-bicity, strongly affect the protein adsorption behavior. Calculated... 

An understanding of protein adsorption behavior is applicable in numerous fields including blood-synthetic materials interfaces, macromolec-ular-rnembrane interactions, receptor interactions, enzyme engineering, adhesion, and protein separation on chromatographic supports. Many methods have evolved to study interfacial adsorption, but no single independent method seems adequate. The ideal technique should produce quantitative, real-time, in situ data concerning the amount, activity, and conformation of proteins adsorbed on well-characterized surfaces. All adsorption techniques are approximations to this optimum. 

One might speculate on a number of chemical and physical factors that govern protein adsorption behavior. Previous experiments point to the importance of hydrophilicity as an influential factor (6), but this is certainly not the sole factor. In this polymer system, hydrophilicity (as governed by the surface concentration of HEM A) increases linearly with the bulk HEM A composition (11). The surface of a protein which is also soluble in aqueous media is probably of a polar nature. If protein adsorption could be characterized by polar interactions, then an adsorption trend that would parallel the... 

The TIRF technique has been refined in this laboratory to provide reproducible results about protein adsorption phenomena at solid-liquid interfaces (17-19). The investigation of protein adsorption behavior using TIRF in this laboratory is discussed below. The overall goal of this research is a complete, general description of the protein adsorption process. 

The stmctural and conformational analysis of proteins adsorbed to solid surfaces is difficult because most common analytical methods are not compatible with the presence of the interacting solids. With recent developments in instrumentation and techniques, our understanding of protein adsorption behavior has improved considerably [4, 14]. The most commonly used techniques include attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR), radiolabeling techniques, immunofluorescence enzyme-linked immunosorbent assay (ELISA), ellipsometry, circular dichroism (CD) spectroscopy, surface plasmon resonance (SPR), and amide HX with nuclear magnetic resonance (NMR). Atomic force microscopy (AFM) and scanning... 

An R, Zhuang W, Yang ZH, et al Protein adsorption behavior on mesoporous titanium dioxide determined by geometrical topography, Chem Eng Set 117 146—155, 2014. 

Protein-adsorption behavior tvas also investigated by in situ spectroscopic ellips-ometry using a rotating compensator apparatus [56]. A fixed angle of incidence of 75° tvas used over a spectrum range of 191 to 1690 nm. The refractive indices of the polymer and the adsorbed protein layer as transparent materials were described using the Cauchy relationship. The thickness (d) and refractive index (n) of the adsorbed protein determined were used to calculate the surface concentration of protein (F) using De Feijter s formula ... 

The goal in this work was to lay out a model complex enough to describe protein adsorptive behavior at hydrophobic solid-water interfaces, but not so intricate as to lose track of surface and molecular property influences on the observed phenomena. 

One should be very cautious about explaining protein adsorption behavior on hydrophilie surfaces the relatively higher value of for jS-easein on the hydrophilie surfaee may be... 

From the result of contact angle measurements, it was expected that there would be no significant difference between PAS and SILASTIC 500-1 in the BSA adsorption and the cell adhesion. In the BSA adsorption test, this expectation seemed to hold. In the cell adhesion experiment, however, the PASs, which showed almost the same protein adsorption behavior, exhibited different cell adhesiveness. The number of adherent cells on PAS-41 and 71 were drastically decreased. Conversely, the numbers of the adherent cells on... 

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