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Protein–Nanoparticle Interactions
Published in Lajos P. Balogh, Nano-Enabled Medical Applications, 2020
Iseult Lynch, Kenneth A. Dawson
The effect of the surface chemistry of biomaterials on the protein adsorption process has been a topic of great interest for many years, and much is known in this field [30]. Protein adsorption to various materials has been widely studied and it has been found that factors such as electrostatic interactions, hydrophobic interactions, and specific chemical interactions between the protein and the adsorbent play important roles. Selective adsorption of proteins on various synthetic adsorbents has been examined under different conditions (such as solution pH and protein concentration) and for many proteins the mechanism of selective adsorption has been attributed to electrostatic interactions [12].
Nanosuspensions as Nanomedicine: Current Status and Future Prospects
Published in Debarshi Kar Mahapatra, Sanjay Kumar Bharti, Medicinal Chemistry with Pharmaceutical Product Development, 2019
Shobha Ubgade, Vaishali Kilor, Abhay Ittadwar, Alok Ubgade
The correlation between in vitro and in vivo performance of nanosuspension formulation and monitoring in-vivo performance is a very critical parameter. The extent of tissue distribution and interaction with plasma proteins has pronounced effect on in-vivo performance of the formulation and this, in turn, depends on the surface properties of the drug like surface hydrophobicity [22]. Techniques such as hydrophobic interaction chromatography can be used to determine surface hydrophobicity [87], whereas 2-D PAGE [88] can be employed for the quantitative and qualitative measurement of protein adsorption after intravenous injection of drug nanosuspensions.
Selection of Material for Dialysis Membrane
Published in Sirshendu De, Anirban Roy, Hemodialysis Membranes, 2017
It is well reported that protein adsorption is primarily due to hydrophobic surfaces. In an aqueous system, initial surface hydration of hydrophobic material governs the subsequent protein adsorption.9 Hydrated protein molecules displace interfacial water via electrostatic interaction, thereby achieving thermodynamic equilibrium.20 , 21 In the direct method, it was observed (Figure 4.19) that S3 exhibited the highest protein adsorption (30 μg/cm2) due to higher hydrophobicity of the membrane (contact angle 80°). Similarly, S2 and S1 membranes exhibit the protein adsorption results in accordance with their degrees of hydrophobicity. S2 (73°) has higher contact angle than S1 (69°) and hence exhibits higher protein adsorption (20 μg/cm2) than S1 (10 μg/cm2).
Protein-liposome interactions: the impact of surface charge and fluidisation effect on protein binding
Published in Journal of Liposome Research, 2023
Efstathia Triantafyllopoulou, Natassa Pippa, Costas Demetzos
In our previous work, we introduced the fraction of stealthiness (Fs) parameter and correlated it with concentration and lipid composition. In this study, we tried to confirm the influence of these factors in protein adsorption and examine the impact of surface charge and fluidity on the extent of protein binding. Fraction of stealthiness values near 0 indicates that liposomes adsorb extensively proteins, whilst Fs value equal to 1 is accompanied by liposomal stealth properties. Firstly, none of our systems lead to Fs values near 1 compared to our previous study. These stealth systems were generally in concentration C = 10 mg/ml, whereas in this study the concentration is 30 mg/ml for all formulations. That confirms the magnitude of concentration. Lower values for systems with the same lipid composition and concentration may reflect differences in incubation protocol. Moreover, the surface charge does have a crucial role, as cationic liposomes exhibit the lowest Fs values, while negatively charged formulations have the highest values. In the matter of fluidisation effect, bare liposomes with less fluid bilayer according to DSC results, lead to lower Fs values. In addition, HSPC and DSPC liposomes with close Tm values and bilayer fluidity show similar protein adsorption. However, considering the behaviour of liposomes in serum, the presence of charge and/or PEGylation seems to mask on fluidisation effect. Interestingly, an increase in the fluidity of liposomes with different main lipids suggests smaller differences in Fs values between liposomes of the same main lipid regardless of surface charge or PEGylation.
Localized, on-demand, sustained drug delivery from biopolymer-based materials
Published in Expert Opinion on Drug Delivery, 2022
Junqi Wu, Sawnaz Shaidani, Sophia K. Theodossiou, Emily J. Hartzell, David L. Kaplan
Effectively delivering therapeutics alongside treated cells may enhance clinical feasibility of local drug delivery. Small-interfering RNA (siRNA) delivery has been shown to reduce fibrosis by downregulating collagen expression [157,158]. Another consideration is blocking protein adsorption using drugs, rather than materials. While anti-protein adsorption materials have been used successfully in medical implants, they are less effective in small drug-delivery polymer systems. Using a drug to block protein adsorption and prevent capsule formation could delay or prevent FBR. Such a drug could be delivered alongside anti-inflammatory substances and the desired therapeutic; however, protein adsorption has also been shown to be necessary for preventing nonspecific cellular uptake of nanocarriers [159]. More work is needed to understand how to control protein adsorption with positive therapeutic outcomes during local drug delivery.
Development of an enzymatic method for the evaluation of protein deposition on contact lenses
Published in Biofouling, 2022
Protein adsorption to surfaces is common in many biological processes (Wang et al. 2012; Firkowska-Boden et al. 2018) and their adsorption to biomaterials in the body can trigger adhesion of particles, bacteria or cells, possibly promoting inflammatory cascades or fouling processes (Taylor et al. 1998; Tan et al. 2002; Rabe et al. 2011; Vijay et al. 2012). When a contact lens is placed in the eye, proteins are immediately adsorbed to it (Lin et al. 1991; Keith et al. 2003; Subbaraman et al. 2006; Hall et al. 2013). Protein adsorption on contact lenses may cause changes in visual acuity and result in complications such as discomfort and dryness (Castillo et al. 1985; Sack et al. 1987). These complications may lead to discontinuation from contact lens wear (Richdale et al. 2007). Therefore, it is important to clearly understand the pattern of deposits.