Deciphering the mechanistic insight into the stoichiometric ratio dependent behavior of Cu(II) on BSA fibrillation

Singh, Ajeet Pal; Datta, P. K.; Pandey, Lalit M.

doi:10.1016/j.ijbiomac.2017.01.045

Cited by 16 publications

(3 citation statements)

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“…During competitive protein adsorption, the interprotein interaction was analyzed so as to determine whether the adsorption process was enthalpy- or entropy-driven. The protein–protein interaction was analyzed by isothermal titration calorimetry using MicroCal iTC-200 (MicroCal, Northampton, MA) at 300 K. It is widely used to determine thermodynamic parameters such as binding constant ( K b ), binding stoichiometry ( n ), and the enthalpy (Δ H ) and entropy (Δ S ) change for the system . All of the protein solutions were prepared in PBS (pH 7.4) to minimize the dilution heat contribution and degassed prior to experiments.…”

Section: Methodsmentioning

confidence: 99%

“…The protein−protein interaction was analyzed by isothermal titration calorimetry using MicroCal iTC-200 (MicroCal, Northampton, MA) at 300 K. It is widely used to determine thermodynamic parameters such as binding constant (K b ), binding stoichiometry (n), and the enthalpy (ΔH) and entropy (ΔS) change for the system. 42 All of the protein solutions were prepared in PBS (pH 7.4) to minimize the dilution heat contribution and degassed prior to experiments. For BSA/FB and BSA/IgG interaction experiments, the FB and IgG concentration was fixed at 0.02 mM and were titrated with BSA (0.4 mM) solution.…”

Section: Isothermal Titration Calorimetry (Itc)mentioning

confidence: 99%

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Conformational and Organizational Insights into Serum Proteins during Competitive Adsorption on Self-Assembled Monolayers

2018

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Physicochemical interactions of proteins with surfaces mediate the interactions between the implant and the biological system. Surface chemistry of the implant is crucial as it regulates the events at the interface. The objective of this study was to explore the performance of modified surfaces for such interactions relevant to various biomedical applications. Because of a wide range of surface wettability, we aimed to study protein behavior (i.e., conformational changes and their packing) during competitive protein adsorption. Three serum proteins (bovine serum albumin, BSA; fibrinogen, FB; and immunoglobulin G, IgG) were tested for their conformational changes and orientation upon adsorption on hydrophilic (COOH and amine), moderately hydrophobic (mixed and hybrid), and hydrophobic (octyl) surfaces generated via silanization. Modified surfaces were characterized using Fourier-transform infrared spectroscopy, contact angle, and atomic force microscopy (AFM) techniques. Adsorbed masses of proteins from single and binary protein solutions on different surfaces were quantified along with their secondary structure analyses. Maximum adsorbed protein masses were found to be on negatively charged and hydrophobic (octyl) surfaces because of ionic and hydrophobic interactions between protein molecules and surfaces, respectively. Side-on and end-on orientations of adsorbed protein molecules were analyzed using theoretical and AFM analyses. We observed compact and elongated forms of BSA molecules on hydrophilic and hydrophobic surfaces, respectively. We further found a linear increase in the α-helix content of BSA and β-sheet contents of FB and IgG proteins with the increasing side-on (%)-oriented protein molecules on the surfaces. This indicates that side-on orientations of adsorbed FB and IgG lead to the formation of β-sheets. Sodium dodecyl sulfate polyacrylamide gel electrophoresis was employed to quantify the protein types and their ratio in competitively adsorbed proteins on different surfaces. A theoretical analysis was also used to determine the % secondary structures of competitively adsorbed proteins from BSA/FB and BSA/IgG solutions, which very well agreed with experimental results. The competitive protein adsorption from both BSA/FB and BSA/IgG solutions was found to be entropy-driven, as revealed by thermodynamic studies performed using isothermal titration calorimetry.

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Section: Methodsmentioning

confidence: 99%

Section: Isothermal Titration Calorimetry (Itc)mentioning

confidence: 99%

Conformational and Organizational Insights into Serum Proteins during Competitive Adsorption on Self-Assembled Monolayers

2018

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“…In an effort to replicate the natural bone structure, researchers have conducted experiments involving the incorporation of various elements into the HAp matrix. The effectiveness of an in vivo implant may be influenced by the fact that these metal ions are also essential for protein aggregation [ 25 ]. The Ca 2+ ions in the crystal lattice of HAp can be substituted by different ions such as Al 3+ , Fe 3+ , Zn 2+ , Ni 2+ , Na + , etc.…”

Section: Introductionmentioning

confidence: 99%

Enhancement of antimicrobial properties by metals doping in nano-crystalline hydroxyapatite for efficient biomedical applications

Habib,

Disha,

Sahadat Hossain

et al. 2024

Heliyon

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Silk Hydrogel Microfibers for Biomimetic Fibrous Material Design

Bradner

McGill

Golding

et al. 2019

Macro Materials & Eng

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Fiber units are conserved design motifs that bestow intrinsic stiffness to biological tissues. Collagen fibrils are the fundamental unit of fibrous tissues with controlled assembly and multiscale structure‐function properties. Characteristic non‐linear tissue response is afforded through energy dissipation at the stiff‐soft interfaces of fibril collagen and extrafibrillar matrix components. The goal of this research is to develop a 3D silk hydrogel microfiber platform with bioinspired toughening mechanisms. Batch fabrication and post‐processing renders fibers that can be handled and with tunable features, as well as loading of components to improve material responses. Matrix loading of a glycoprotein, bovine serum albumin (BSA), adds a primary defense mechanism to material failure in the form of sacrificial bonds. This enables nano‐ to micro‐scale rearrangement with strain and improved fiber toughness compared to silk‐only fibers. Further biomimicry is added via matrix loading of a biosilica precursor peptide, R5, enabling biomineralization in the form of silicification. Inorganic mineral deposition of Silk‐BSA‐R5 hydrogel microfibers provides a fibrous scaffold for applications that require fibril‐mineral interfaces for load transduction. This microfiber platform introduces a methodology for meticulous fibrous scaffold design with biomimetic fibril hierarchy, toughening mechanisms, and loading capabilities for systematic tissue engineering applications.

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Deciphering the mechanistic insight into the stoichiometric ratio dependent behavior of Cu(II) on BSA fibrillation

Cited by 16 publications

References 50 publications

Conformational and Organizational Insights into Serum Proteins during Competitive Adsorption on Self-Assembled Monolayers

Conformational and Organizational Insights into Serum Proteins during Competitive Adsorption on Self-Assembled Monolayers

Enhancement of antimicrobial properties by metals doping in nano-crystalline hydroxyapatite for efficient biomedical applications

Silk Hydrogel Microfibers for Biomimetic Fibrous Material Design

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