Revealing fibrinogen monolayer conformations at different pHs: Electrokinetic and colloid deposition studies

Revealing deposition mechanism of colloid particles on human serum albumin monolayers

“…at the same pH of 3.5 are also plotted in Fig. 6 [40]. One can observe that in this case the critical value of h m is equal to 75 nm that agrees with the the extended length of the fibrinogen molecule predicted at this pH [44].…”

“…3a were quantitative interpreted in terms of the random sequential adsorption (RSA) approach used before for modeling the deposition of colloid particles at surface covered by polyelectrolyte [39] and fibrinogen molecules [40]. Using the RSA modeling an analytical expressions has been derived for calculating the deposition probability of colloid particles in terms of their coverage and the protein surface concentration.…”

“…These theoretical results were calculated according to the method described in Ref. [40,42] by considering the electrostatic interactions between the particles and mica covered by HSA using the meanfield values of zeta potentials (see Fig. 2).…”

“…This effect can be quantitatively analyzed by determining the minimum approach distance, denoted by h m , as a function of ionic strength. This is done according to the method developed in Ref [40,42],. by assuming that the particle/mica net interaction energy is thesum the electrostatic and the van der Waals interactions.…”

Self-assembled fibrinogen–fibronectin hybrid protein nanofibers with medium-sensitive stability

“…Changes in surface charge of a protein and thus z Pot may imply protein unfolding and/or aggregation. 18,46,47 Therefore, the variation in the z Pot as a function of ber composition can be corroborated to changes in hPNFs surface charge due to various degrees of protein unfolding and thus the amount of amino acid sequences exposed by the proteins.…”