Browse
Submit Data
Databases
API
Help

Dataset Information

6 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

A one-step method for covalent bond immobilization of biomolecules on silica operated in aqueous solution.

ABSTRACT: A simple, one-step method for covalent bond immobilization of biomolecules on silica operated in water is described. In the approach, an NHS-ester linked methallylsilane is utilized as a bifunctional linker to couple the biomolecule to the silica surface. Weak organic acid such as acetic acid activates the silica surface enough to react with bifunctional linker without destroying activity of biomolecule.

SUBMITTER: Sim YK

PROVIDER: S-EPMC6201817 | biostudies-other | 2018 Nov

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Publications

A one-step method for covalent bond immobilization of biomolecules on silica operated in aqueous solution.

Sim Yong-Kyun YK Jung Heetae H Kim Su Hyun SH Park Jung-Woo JW Park Woo-Jin WJ Jun Chul-Ho CH

Chemical science 20180824 41

A simple, one-step method for covalent bond immobilization of biomolecules on silica operated in water is described. In the approach, an NHS-ester linked methallylsilane is utilized as a bifunctional linker to couple the biomolecule to the silica surface. Weak organic acid such as acetic acid activates the silica surface enough to react with bifunctional linker without destroying activity of biomolecule. ...[more]

PMID: 30430001

Similar Datasets

Rapid one-step 18F-radiolabeling of biomolecules in aqueous media by organophosphine fluoride acceptors.

Project description:Currently, only a few 18F-radiolabeling methods were conducted in aqueous media, with non-macroelement fluoride acceptors and stringent conditions required. Herein, we describe a one-step non-solvent-biased, room-temperature-driven 18F-radiolabeling methodology based on organophosphine fluoride acceptors. The high water tolerance for this isotope-exchange-based 18F-labeling method is attributed to the kinetic and thermodynamic preference of F/F over the OH/F substitution based on computational calculations and experimental validation. Compact [18/19F]di-tert-butyl-organofluorophosphine and its derivatives used as 18F-labeling synthons exhibit excellent stability in vivo. The synthons are further conjugated to several biomolecular ligands such as c(RGDyk) and human serum albumin. The one-step labeled biomolecular tracers demonstrate intrinsic target imaging ability and negligible defluorination in vivo. The current method thus offers a facile and efficient 18F-radiolabeling pathway, enabling further widespread application of 18F.

| S-EPMC6397219 | biostudies-literature

One-step acquisition of functional biomolecules from tissues.

Project description:Direct determination of functional biomolecular chemistry of clinically relevant tissues in vivo is a challenging task. Current approaches, based on tissue retrieval by biopsy and subsequent solubilization, are limited in terms of accurate representation of tissue constituents, reproducibility, and retention of functionality of solubilized tissue biomolecules. Using a pool of known surfactants, we designed and screened a large combinatorial library of surfactant formulations, which led to the discovery of rare synergistic formulations that greatly enhance tissue solubilization as well as preserve bioactivity of solubilized molecules, in particular proteins. By combining these formulations with a short ultrasound application, we developed a tissue sampling method--STAMP (Surfactant-based Tissue Acquisition for Molecular Profiling)--for rapid one-step determination of functional tissue chemistry in vivo. We specifically demonstrate STAMP-assisted profiling of a multitude of proteins, lipids, and genomic DNA in skin and mucosal tissues. Applications of this sampling methodology to rapid molecular diagnostics of cutaneous allergies and infectious diseases are also presented.

| S-EPMC2930427 | biostudies-literature

Chromium removal from aqueous solution by a PEI-silica nanocomposite.

Project description:It is essential and important to determine the adsorption mechanism as well as removal efficiency when using an adsorption technique to remove toxic heavy metals from wastewater. In this research, the removal efficiency and mechanism of chromium removal by a silica-based nanoparticle were investigated. A PEI-silica nanoparticle was synthesized by a one-pot technique and exhibited uniformly well-dispersed PEI polymers in silica particles. The adsorption capacity of chromium ions was determined by a batch adsorption test, with the PEI-silica nanoparticle having a value of 183.7?mg/g and monolayer sorption. Adsorption of chromium ions was affected by the solution pH and altered the nanoparticle surface chemically. First principles calculations of the adsorption energies for the relevant adsorption configurations and XPS peaks of Cr and N showed that Cr(VI), [HCrO4]- is reduced to two species, Cr(III), CrOH2+ and Cr3+, by an amine group and that Cr(III) and Cr(VI) ions are adsorbed on different functional groups, oxidized N and NH3+.

| S-EPMC5780388 | biostudies-literature

Stimulus-responsive controlled release system by covalent immobilization of an enzyme into mesoporous silica nanoparticles.

Project description:Mesoporous silica nanoparticles (MSN) have emerged as an attractive class of drug delivery carriers for therapeutic agents. Herein, we explored the covalent immobilization of proteins into MSN to generate a stimulus-responsive controlled release system. First, MSN were functionalized with thiol groups using (mercaptopropyl)-trimethoxysilane (MPTMS). Functionalization was verified by X-ray photoelectron spectroscopy (XPS), Fourier-transform infrared (FTIR) spectroscopy, and dynamic light scattering. The model enzyme carbonic anhydrase (CA) was coupled to sulfosuccinimidyl 6-[3'(2-pyridyldithio)-propionamido]hexanoate (Sulfo-LC-SPDP) at a low ratio of 1:1 to prevent enzyme inactivation and subsequently covalently immobilized into MSN via thiol-disulfide interchange. The enzyme could be released from MSN with 10 mM glutathione, which represents intracellular redox conditions, while it remained bound to the MSN at extracellular redox conditions represented by 1 ?M glutathione. The activity of the released enzyme was >80% demonstrating that the enzyme was still largely functional and active after immobilization and release. Human cervical cancer (HeLa) cells were incubated with the MSN-CA bioconjugates at various concentrations for 24 h and the data show good biocompatibility. In summary, we demonstrate the potential of MSN as drug delivery systems for proteins.

| S-EPMC3329583 | biostudies-literature

Targeting biomolecules with reversible covalent chemistry.

Project description:Interaction of biomolecules typically proceeds in a highly selective and reversible manner, for which covalent bond formation has been largely avoided due to the potential difficulty of dissociation. However, employing reversible covalent warheads in drug design has given rise to covalent enzyme inhibitors that serve as powerful therapeutics, as well as molecular probes with exquisite target selectivity. This review article summarizes the recent advances in the development of reversible covalent chemistry for biological and medicinal applications. Specifically, we document the chemical strategies that allow for reversible modification of the three major classes of nucleophiles in biology: thiols, alcohols and amines. Emphasis is given to the chemical mechanisms that underlie the development of these reversible covalent reactions and their utilization in biology.

| S-EPMC5107367 | biostudies-literature

Silica encapsulation of thiol-stabilized lead selenide (PbSe) quantum dots in aqueous solution.

Project description:Silica encapsulation of lead selenide quantum dots (PbSe QDs) in aqueous solution is reported. Thioglycolic acid (TGA) stabilized PbSe QDs were modified with 3-mercaptopropyl trimethoxysilane (MPS) through vigorous stirring in water for 18-24 h in alkaline solution (pH 10.4-10.6). Silica shell was developed by controlled deposition and precipitation of silicates from sodium silicate solution onto MPS modified QDs surfaces. TEM images showed multiple PbSe QDs encapsulated in silica shell. The size of PbSe-SiO2 core-shell nanocrystals was estimated to be 25-30 nm by TEM. Elemental compositions (Pb, Se and Si) were investigated by EDX analysis. The purified colloids of PbSe-SiO2 QDs were stable for months when kept at 4 °C.

| S-EPMC3665949 | biostudies-literature

Removal of Cr(VI) from Aqueous Solution by Polypyrrole/Hollow Mesoporous Silica Particles.

Project description:Abstract: The removal of Cr(VI) in wastewater plays an important role in human health and environment. In this work, polypyrrole/hollow mesoporous silica particle (PPy/HMSNs) adsorbents have been newly synthesized by in-situ polymerization, which prevent the aggregation of pyrrole in the process of polymerization and exhibit highly selective and powerful adsorption ability for Cr(VI). The adsorption process was in good agreement with the quasi-second-order kinetic model and the Langmuir isotherm model. And the maximum adsorption capacity of Cr(VI) was 322 mg/g at 25 °C. Moreover, the removal rate of Cr(VI) by PPy/HMSNs was ~100% in a number of binary systems, such as Cl-/Cr(VI), NO3-/Cr(VI), SO42-/Cr(VI), Zn2+/Cr(VI), Fe3+/Cr(VI), Sn4+/Cr(VI), and Cu2+/Cr(VI). Thus, the PPy/HMSNs adsorbents have great potential for the removal of Cr(VI) in wastewater.

| S-EPMC7221785 | biostudies-literature

Novel Application of Magnetic Protein: Convenient One-Step Purification and Immobilization of Proteins.

Project description:Recently, a magnetic protein was discovered, and a multimeric magnetosensing complex was validated, which may form the basis of magnetoreception. In this study, the magnetic protein was firstly used in biotechnology application, and a novel convenient one-step purification and immobilization method was established. A universal vector and three linker patterns were developed for fusion expression of magnetic protein and target protein. The magnetic protein was absorbed by iron beads, followed by target protein aggregation, purification, and immobilization. GFP, employed as a reporter protein, was successfully purified from cell lysate. Subsequently, three enzymes (lipase, ?-L-arabinofuranosidase, pullulanase) with different molecular sizes testified the versatility of this magnetic-based approach. The specific activities of the purified enzymes were distinctly higher than those of the traditionally purified enzymes using affinity chromatography. The lipase immobilized on iron beads presented improved thermostability and enhanced pH tolerance compared to the free enzyme. The immobilized lipase could be easily recovered and reused for maximum utilization. After 20 cycles of reutilization, the magnetically immobilized lipase retained 71% of its initial activity. This investigation may help introduce magnetic protein into biotechnology applications, and the one-step purification and immobilization method may serve to illustrate an economically viable process for industry.

| S-EPMC5645317 | biostudies-literature

Highly Efficient One-Step Protein Immobilization on Polymer Membranes Supported by Response Surface Methodology.

Project description:Immobilization of proteins by covalent coupling to polymeric materials offers numerous excellent advantages for various applications, however, it is usually limited by coupling strategies, which are often too expensive or complex. In this study, an electron-beam-based process for covalent coupling of the model protein bovine serum albumin (BSA) onto polyvinylidene fluoride (PVDF) flat sheet membranes was investigated. Immobilization can be performed in a clean, fast, and continuous mode of operation without any additional chemicals involved. Using the Design of Experiments (DoE) approach, nine process factors were investigated for their influence on graft yield and homogeneity. The parameters could be reduced to only four highly significant factors: BSA concentration, impregnation method, impregnation time, and electron beam irradiation dose. Subsequently, optimization of the process was performed using the Response Surface Methodology (RSM). A one-step method was developed, resulting in a high BSA grafting yield of 955 mg m-2 and a relative standard deviation of 3.6%. High efficiency was demonstrated by reusing the impregnation solution five times consecutively without reducing the final BSA grafting yield. Comprehensive characterization was conducted by X-ray photoelectron spectroscopy (XPS), Fourier-transform infrared spectroscopy (FTIR), and measurements of zeta potential, contact angle and surface free energy, as well as filtration performance. In addition, mechanical properties and morphology were examined using mercury porosimetry, tensile testing, and scanning electron microscopy (SEM).

| S-EPMC8804297 | biostudies-literature

One-step interfacial synthesis and assembly of ultrathin luminescent AuNPs/silica membranes.

Project description:A facile one-step strategy is explored to achieve uniform luminescent Au nanoparticles (AuNPs) in a two-dimensional ultrathin silica matrix based on simultaneous reaction and assembly at the liquid-liquid interface. The as-prepared AuNPs/silica nanocomposites can be further employed to fabricate micrometer-thick films with bifunctional luminescent and superhydrophobic properties. Such a versatile concept is ideal for the development of multifunctional devices.

| S-EPMC3574619 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data