Protein adsorption kinetics

Ramsden J J 1994 Experimental methods for investigating protein adsorption kinetics at surfaces Q. Rev. Blophys. 27 41-105... 

Van Tassel P R, Guemourl L, Ramsden J J, Tar]us G, VIot P and Talbot J 1998 A model for the Influence of conformational change on protein adsorption kinetics J. Colloid Interfaoe Sc/. 207 317-23... 

A useful literature relating to polypeptide and protein adsorption kinetics and equilibrium behavior in finite bath systems for both affinity and ion-ex-change HPLC sorbents is now available160,169,171-174,228,234 319 323 402"405 and various mathematical models have been developed, incorporating data on the adsorption behavior of proteins in a finite bath.8,160 167-169 171-174 400 403-405 406 One such model, the so-called combined-batch adsorption model (BAMcomb), initially developed for nonporous particles, takes into account the dynamic adsorption behavior of polypeptides and proteins in a finite bath. Due to the absence of pore diffusion, analytical solutions for nonporous HPLC sorbents can be readily developed using this model and its two simplified cases, and the effects of both surface interaction and film mass transfer can be independently addressed. Based on this knowledge, extension of the BAMcomb approach to porous sorbents in bath systems, and subsequently to packed-, expanded-, and fluidized-bed systems, can then be achieved. 

Ramsden, J.J. et al., Protein adsorption kinetics drastically altered by repositioning a single charge, J. Am. Chem. Soc., 117, 8511, 1995. 

There is one more peculiarity in protein adsorption kinetics which is worthy of note. As shown in Fig. 5.42 (Miller et al. 1993a) slight compressions of the adsorption layers of a 0.1 mg/ml HA solution surprisingly lead to surface tensions as low as 42 mN/m, although the lowest equilibrium surface tension at 50 mg/ml amoimts to about 52 mN/m. 

Protein Adsorption and Desorption Rates and Kinetics. The TIRF flow cell was designed to investigate protein adsorption under well-defined hydrodynamic conditions. Therefore, the adsorption process in this apparatus can be described by a mathematical convection-diffusion model (17). The rate of protein adsorption is determined by both transport of protein to the surface and intrinsic kinetics of adsorption at the surface. In general, where transport and kinetics are comparable, the model must be solved numerically to yield protein adsorption kinetics. The solution can be simplified in two limiting cases 1) In the kinetic limit, the initial rate of protein adsorption is equal to the intrinsic kinetic adsorption rate. 2) In the transport limit, the initial protein adsorption rate, as predicted by Ldveque s analysis (23), is proportional to the wall shear rate raised to the 1/3 power. In the transport-limited adsorption case, intrinsic protein adsorption kinetics are unobservable. 

Norde W, Rouwendal E (1990) Streaming potential measurements as a tool to study protein adsorption-kinetics. J Colloid Interface Sd 139(1) 169-176... 

Equation (173) derived for no blocking effects apparently resembles the Langmuir model widely used for the interpretation of particle and protein adsorption kinetics [1,8,120-122]. In accordance with this model, one postulates that the adsorption flux is reduced by the factor 1 — 0/0 , where is the maximum coverage, usually found empirically. Using this hypothesis, one can formulate Eq. (172) as... 

Kidane et al. [22] studied protein adsorption kinetics on polyethylene oxide (PEO)-grafted glass. Results showed that protein adsorption on PEO-grafted glass reached its equilibrium state rapidly. Shibata and Lenhoff [23] used the total internal reflectance fluorescence (TIRE) spectroscopy to determine the kinetics of protein adsorption on modified (butylated or amino-propylated) quarte surfaces. They found that the rate constant under a given set of conditions appeared to be correlated with the ultimate extent of adsorption observed imder those conditions. 

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