Unraveling the binding mechanism of polyoxyethylene sorbitan esters with bovine serum albumin: A novel theoretical model based on molecular dynamic simulations

Key interactions of surfactants in therapeutic protein formulations: A review

“…It was also recently shown that PEO chains can also exhibit affinity for proteins like BSA [62]. Delgado et al [63] support this hypothesis with their molecular dynamics simulation results, which suggest enhanced stabilization of BSA by cooperative self-assembly with polysorbate molecules. However, Hoffman et al …”

In Vitro Drug and Gene Delivery Using Random Cationic Copolymers Forming Stable and pH‐Sensitive Polymersomes

“…This can be attributed to the large mPEG content in the polymeric backbone of CP11 polymer. Indeed, mPEG is known to reduce interaction of polymers with the albumin protein . It should be noted that at the highest experimental concentration ( C p = 2.0 mg mL −1 ) of all the polymers, the α‐helix content is only slightly reduced with respect to that of pure HSA, indicating denaturation of the native structure of the protein.…”

“…Indeed, mPEG is known to reduce interaction of polymers with the albumin protein. [65] It should be noted that at the highest experimental concentration (C p = 2.0 mg mL −1 ) of all the polymers, the α-helix content is only slightly reduced with respect to that of pure HSA, indicating denaturation of the native structure of the protein. Since the polymers do not have any denaturing effect on the secondary structure of the carrier protein HSA in the cell viable concentration range, they may find application as a potential intravenous DDS.…”

Interaction of biocompatible sugar based surfactant n-dodecyl β-d-maltoside with lysozyme

“…Protein-surfactant interactions have been widely studied because they are important in a wide variety of industrial, biological, pharmaceutical, and cosmetic systems [3,4]. Binding of the surfactants to the proteins can lead to the conformational changes of the macromolecules which generally results in the changes of polarity and stability of the protein [3][4][5][6][7][8][9].…”

“…These surfactants possess some interesting properties, distinct from those of conventional ones, because of their multi-functionality and presence of a large, relatively rigid (sugar) head-group. The interaction of the surfactants, either synthetic as well as obtained from the petroleum industries, with proteins is abundant in literature [3][4][5][6][7][8][9][11][12][13][14][15]; however, the work related to the non-toxic biodegradable surfactants is limited [16][17][18]. Therefore, we have studied the interaction between n-dodecyl β-D-maltoside (C 12 G 2 ), a sugar-based surfactant, and lysozyme (Scheme 1), a well known enzymatic protein by using a bunch of techniques such as surface tensiometry, synchronous and intrinsic fluorescence, circular dichroism (CD), Fourier-transform infra-red (FTIR), dynamic light scattering (DLS), and UV-visible absorption spectroscopies.…”