Protein mixtures of environmentally friendly zein to understand protein–protein interactions through biomaterials synthesis, hemolysis, and their antimicrobial activities

Abstract

Industrially important zein protein has been employed to understand its interactions with two model proteins bovine serum albumin (BSA) and cytochrome c (Cyc,c) following the in vitro synthesis of Au NPs so as to expand its applicability for biological applications. Interactions were studied under the effect of temperature variation by UV-visible and fluorescence emission studies. Temperature induced unfolding in the protein mixtures indicated their degree of mutual interactions through simultaneous nucleation of gold nanoparticles (Au NPs) and their subsequent shape control effects. Zein + BSA mixtures showed favorable protein-protein interactions over the entire mole fraction range with maximum close to x(BSA) = 0.24, whereas zein + Cyc,c showed such interactions only in the zein rich region with significant demixing in the Cyc,c rich region of the mixtures. Both hydrophobic as well as hydrophilic domains in the unfolded states were driving such interactions in the case of zein + BSA mixtures while demixing was the result of the predominant hydrophilic nature of Cyc,c and its self-aggregation behavior in the Cyc,c rich region in contrast to the predominant hydrophobic nature of zein. Zein + BSA mixtures produced small roughly spherical Au NPs fully coated with protein, whereas the demixing zone of zein + Cyc,c mixtures generated highly anisotropic NPs with little protein coating. To explore their biological applications, protein conjugated NPs of both mixtures were subjected to hemolysis where NPs coated with the former mixture showed little hemolysis and may act as drug delivery vehicles in systemic circulation in comparison to the latter. Both kinds of NPs further demonstrated their extraordinary antimicrobial activities with different kinds of strains and proved to be highly important environmentally friendly biomaterials.

Volumetric, ultrasonic and UV absorption studies on interactions of antibiotic drug chloramphenicol with glycine and its dipeptide in aqueous solutions at T = (288.15–318.15) K

“…A vital role is played by drug-protein interactions in all the metabolic pathways or biological processes occurring inside the body. Study of these interactions led to modern drug discovery for conceding target proteins through which biological molecules betray their pharmacological actions [32,33]. So the recognition of drugs in aqueous and non-aqueous solutions have evoked a lot of interest because their activities involve interaction with biological membranes [34][35][36][37][38].…”

Fluorescent Schiff base sensors as a versatile tool for metal ion detection: strategies, mechanistic insights, and applications

“…3.4.3 Drug sample analysis. The improvement in the field of analytical chemistry is supported by the use of fluorescent materials, 170 biomaterials, 271,272 and nanomaterials [273][274][275] in the analysis of samples. Fluorescent materials offer various advantages such as fast analysis time, high sensitivity and selectivity, low detection limit, and in vivo and in vitro investigation facility.…”

Nanoparticle Surface Specific Adsorption of Zein and Its Self-assembled Behavior of Nanocubes Formation in Relation to On–Off SERS: Understanding Morphology Control of Protein Aggregates

“…This allows a favorable adsorption of zein on growing NPs in the seed−growth method, as evident from Figure 3c. This is not the case when zein is involved in the in situ reaction, where it is first involved in the reduction of Au(III) into Au(0) 30,31 and, then, in the stabilization of the nucleating centers by adsorbing on the NPs surface simply by close Van der waals interactions. 31 Thus, a reduction and stabilization process may cause a drastic decrease in the α-helix structure of zein, and hence, it is not fully resolved, in contrast to the zein adsorbed on growing Au seeds.…”