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Micelles

Micelles are self-assembling aggregates of amphiphilic molecules, such as surfactants or lipids, that form in aqueous solutions.
These nano-scale structures have a hydrophilic exterior and a hydrophobic interior, allowing them to solubilize and transport hydrophobic compounds.
Micelles play a crucial role in various biological and technological applications, including drug delivery, detergency, and nanomaterial synthesis.
Understaning the formation, struction, and properties of micelles is essential for optimizing research protocols and enhancing reproducibility in areas like micellar analysis.
PubCompare.ai's AI-powered platform provides data-driven insights to help researchers locate and compare the best micelle-related protocols from literature, preprints, and patents, experieinceing the future of protocol optimization.

Most cited protocols related to «Micelles»

Reconstitution of CLC-ec1 chloride channel

Cited 18 times

Chemicals and other materials were of reagent quality. Expression, His-tag cleavage, purification, and liposome reconstitution of CLC-ec1, the product of Escherichia coli gene clcA (accession P37019), were performed as previously described (Accardi et al., 2004 (link)), except that for samples used in liposome fluxes, the final purification step was gel filtration on Superdex 200 rather than anion exchange chromatography on Poros HQ, which was used exclusively for planar lipid bilayer experiments. All preparations (typically 1–10 mg/ml in 5–20 mM decylmaltoside) were checked by overloaded SDS-PAGE to be free of His-tagged and other contaminating bands. Point mutants were constructed by conventional PCR methods and were fully sequenced. All mutants reported expressed well (1–3 mg/liter culture) and gave gel filtration profiles identical to the wild-type homodimer.
Liposomes were formed within 1 d of protein preparation by 30-h dialysis of micellar solutions containing E. coli polar lipid (Avanti, 20 mg/ml), detergent (Chaps, 35 mM), and protein (0.03–50 μg/mg lipid). Protein concentration is reported throughout as protein/lipid weight ratio, denoted “protein density.” Liposomes used for planar bilayer recording were prepared at a protein density of 50 μg/mg in 450 mM KCl, 25 mM KH₂PO₄, 22.5 mM K₃-citrate, 2.5 mM citric acid, pH 7.5. Liposomes used for flux measurements were formed with protein at 0.03–5 μg/mg, 300 mM KCl, and buffered with 25 mM citrate for Cl⁻ flux experiments or 25 mM citrate/ 25 mM phosphate (CPi) for H⁺ flux experiments, adjusted with NaOH to the desired pH in the range 4.5–5.5. (Some experiments used 75 mM glutamate as buffer, with similar results.) After dialysis, liposomes were stored in aliquots at −80°C until the day of use.

Walden M., Accardi A., Wu F., Xu C., Williams C, & Miller C. (2007). Uncoupling and Turnover in a Cl−/H+ Exchange Transporter. The Journal of General Physiology, 129(4), 317-329.

Publication 2007

3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Anions Buffers Chromatography Citrates Citric Acid Cytokinesis Detergents Dialysis Dialysis Solutions Escherichia coli Gel Chromatography Glutamates Lipid Bilayers Lipids Liposomes Micelles Phosphates Proteins SDS-PAGE Staphylococcal Protein A

Purification of μOR-Gi-scFv16 Complex

Cited 16 times

Purified DAMGO-bound μOR was mixed with a 1.2 molar excess of
G_i heterotrimer. The coupling reaction was allowed to proceed at
24 °C for 1 hour and was followed by addition of apyrase to catalyze
hydrolysis of unbound GDP, which destabilizes the nucleotide-free
complex⁴⁰. After one
more hour at 25 °C, a 4-fold volume of 20 mM Hepes pH 7.5, 100 mM NaCl,
1% lauryl maltose neopentyl glycol (L-MNG), 0.1% CHS was added
to the complexing reaction to initiate detergent exchange. After one hour
incubation at 25 °C to allow micelle exchange, 1 mM MnCl₂ and
lambda phosphatase (New England Biolabs) were added to dephosphorylate the
preparation. This reaction was further incubated at 4 °C for 2 hours. To
remove excess G protein and residual DDM, the complexing mixture was purified by
M1 anti-FLAG affinity chromatography. Bound complex was first washed in a buffer
containing 1% L-MNG, followed by washes in gradually decreasing L-MNG
concentrations. The complex was then eluted in 20mM Hepes pH 7.5, 100mM NaCl,
0.01% MNG/0.001% CHS, 300 nM DAMGO, 5 mM EDTA, and FLAG peptide.
The eluted complex was supplemented with 100 μM TCEP to provide a
reducing environment. The tobacco etch virus (TEV) protease and human rhinovirus
3C protease were added to cleave the flexible μOR amino- and carboxy-
termini. Finally, a 1.2 molar excess of scFv16 was added to the preparation.
Once cleavage of the termini was confirmed by SDS-PAGE, the
μOR-G_i-scFv16 complex was purified by size exclusion
chromatography on a Superdex 200 10/300 column in 20mM Hepes pH 7.5, 100mM NaCl,
300 nM DAMGO, 0.00075% MNG and 000025% GDN. Peak fractions were
concentrated to ~7 mg/mL for electron microscopy studies.

Koehl A., Hu H., Maeda S., Zhang Y., Qu Q., Paggi J.M., Latorraca N.R., Hilger D., Dawson R., Matile H., Schertler G.F., Granier S., Weis W.I., Dror R.O., Manglik A., Skiniotis G, & Kobilka B.K. (2018). Structure of the μ Opioid Receptor-Gi Protein Complex. Nature, 558(7711), 547-552.

Publication 2018

Apyrase Chromatography, Affinity Complex Mixtures Cytokinesis Detergents Edetic Acid Electron Microscopy Enkephalin, Ala(2)-MePhe(4)-Gly(5)- FLAG peptide Glycols GTP-Binding Proteins HEPES Homo sapiens Maltose manganese chloride Micelles Molar Nucleotides Peptide Hydrolases Phosphoric Monoester Hydrolases SDS-PAGE Sodium Chloride TEV protease tris(2-carboxyethyl)phosphine

Martini Modeling of Lipopolysaccharides in CHARMM-GUI

Cited 16 times

Martini models of two different LPS, Ra LPS (RAMP) and Re LPS (REMP), were added in CHARMM-GUI Martini Maker (Figure 1). The LPS models follow a 4-to-1 mapping scheme of the Martini force field and the parameters were optimized based on united-atom LPS simulations to improve accuracy.^{35 (link),36 (link)}The overall building procedures of all LPS-containing Martini Maker modules (Bilayer/Nanodisc/Vesicle/Micelle/Random Builders) are identical from the original implementation.^{34 (link)} Briefly, in STEP 1, a user-specified protein structure is read-in through PDB Reader. In STEP 2, the protein orientation is changed based on the user-specific input; by definition, the Z axis is the membrane normal and Z = 0 is the membrane center. In STEP 3, the system size is determined, and the pseudo spheres are placed for assigning lipid head group positions. Note that this is the first step when the membrane-only generation option is selected. In STEP 4, the system components (lipids, water, and ions) are generated. Finally, all the components are assembled in STEP 5. During STEP 5, the CHARMM structure (PSF) and coordinate (CRD/PDB) files of each component generated in STEP 4 are merged into single PSF and CRD/PDB files, and water beads in close proximity to the solutes are removed.
Some LPS-specific changes were introduced in the system size calculation and ion placement steps. As described above, the system size was previously determined in STEP 3. However, as the LPS molecule has a long carbohydrate chain, a portion of the LPS molecule can be stretched out beyond the system box determined in STEP 3 based on phospholipids. To resolve this issue, if the system contains LPS, the system size is recalculated by taking the LPS height into account in STEP 4, and the updated system size information is used for further steps (building water box and placing ions).
As divalent cations play an important role in stabilizing the bacterial OM by interacting with the LPS,^{22 (link),37 (link)–40 (link)} the ion placement procedure in STEP 4 was modified to use Ca²⁺ as the counterions for LPS lipid A and core oligosaccharides. By default, CHARMM-GUI adds Ca²⁺ ions to neutralize lipid A, but for the LPS core, CHARMM-GUI provides an option to select an ion type (Na⁺ or Ca²⁺).

Hsu P.C., Bruininks B.M., Jefferies D., de Souza P.C., Lee J., Patel D.S., Marrink S.J., Qi Y., Khalid S, & Im W. (2017). CHARMM-GUI Martini Maker for Modeling and Simulation of Complex Bacterial Membranes with Lipopolysaccharides. Journal of computational chemistry, 38(27), 2354-2363.

Publication 2017

Bacteria Carbohydrates Cations, Divalent Epistropheus Head Lipid A Lipids Micelles Oligosaccharides Phospholipids Proteins Re lipopolysaccharide Tissue, Membrane

Probing EmrE Protein Dynamics by NMR and FRET

Cited 16 times

EmrE was expressed and purified using a 6× His-tag, which was then removed with thrombin. Purification was performed in decylmaltoside (DM) or dodecylmaltoside (DDM). EmrE was reconstituted into dimyristoylphosphatidylcholine (DMPC) or dilauroylphosphatidylcholine (DLPC) liposomes using standard methods and then formed into isotropic bicelles by addition of dihexanoylphosphatidylcholine (DHPC) and several freeze-thaw cycles. Protein concentration was determined using absorbance at 280 nm, with an extinction coefficient determined by amino acid analysis. ITC was performed by titrating 54 μM TPP⁺ stock solutions into 10 μM EmrE, with matching concentrations of detergent or lipid in both solutions.
Bulk FRET labeling was performed in liposomes to separately label residues on either side of the membrane. An “antiparallel” sample was labeled with donor and acceptor on opposite sides and a “parallel” sample was labeled with donor and acceptor on the same side. Donor-only and acceptor-only controls were labeled with dye only on the exterior of the liposome, reconstituted into bicelles and then mixed. Single-molecule FRET samples were labeled in micelles and experiments were performed using a wide-field total internal reflection fluorescence microscope (TIRF) setup^{43 (link)}.
NMR experiments were performed using a 700 MHz Varian NMR spectrometer or 800 MHz Bruker spectrometer equipped with a cryoprobe. All NMR samples contained 0.5–1.0 mM ²H/¹⁵N-EmrE in buffer conditions of 2 mM TPP⁺, 20 mM NaCl, 20 mM potassium phosphate, 2 mM TCEP, pH 7.0, 45°C. The membrane mimetic in each sample (DDM micelles or isotropic bicelles) is as listed. The TROSY-selected ZZ-exchange experiment^{35 (link)} was modified to include a lipid “flipback” pulse. Data were processed and analyzed with NMRPipe^{46 (link)}, NMRView^{47 (link)}, Sparky⁴⁸, and IgorPro (Wavemetrics). All EmrE structure figures were created in PyMOL using PDB 3B5D with the backbone rebuilt to render the cartoons. Full page versions of the spectra in the main figures are included in the supplementary information.

Morrison E.A., DeKoster G.T., Dutta S., Clarkson M.W., Vafabakhsh R., Bahl A., Kern D., Ha T, & Henzler-Wildman K.A. (2011). Antiparallel EmrE exports drugs by exchanging between asymmetric structures. Nature, 481(7379), 45-50.

Publication 2011

1,2-hexanoylphosphatidylcholine Amino Acids Buffers Detergents Dietary Fiber dilauroyl lecithin Dimyristoylphosphatidylcholine dodecyl maltoside Extinction, Psychological Fluorescence Resonance Energy Transfer Freezing Lipids Liposomes Micelles Microscopy, Fluorescence potassium phosphate Proteins Pulse Rate Reflex Sodium Chloride Thrombin Tissue, Membrane Tissue Donors tris(2-carboxyethyl)phosphine Vertebral Column

Purification and Reconstitution of KcsA Ion Channel

Cited 16 times

KcsA was expressed in E. coli and purified on Ni²⁺ affinity columns as described (Heginbotham et al. 1997; MacKinnon et al. 1998). The purified channel was eluted in 400 mM imidazole at 1–5 mg/ml protein concentration quantified by the extinction coefficient at 280 nm (Heginbotham et al. 1998). Immediately after purification, KcsA was reconstituted into liposomes at room temperature as follows. A micellar solution of phospholipids (7.5 mg/ml POPE, 2.5 mg/ml POPG) and 34 mM CHAPS in reconstitution buffer (450 mM KCl/10 mM HEPES/4 mM N-methylglucamine, pH 7.0) was prepared as described (Heginbotham et al. 1998), and KcsA protein was added to final concentrations of 2.5–10 μg/ml, according to the number of channels per liposome desired. After 20–30 min incubation, 400 μl of the mixture was passed down a 20–ml Sephadex G-50 (fine) column equilibrated with reconstitution buffer. Liposomes eluted in the void volume with a dilution of approximately threefold and were stored in 75-μl aliquots at −80°C for up to 3 mo.

Heginbotham L., LeMasurier M., Kolmakova-Partensky L, & Miller C. (1999). Single Streptomyces lividans K+ Channels: Functional Asymmetries and Sidedness of Proton Activation. The Journal of General Physiology, 114(4), 551-560.

Publication 1999

1-palmitoyl-2-oleoylphosphatidylethanolamine 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate ATP8A2 protein, human Buffers Escherichia coli Extinction, Psychological HEPES imidazole Liposomes Meglumine Micelles Phospholipids Proteins sephadex G 50 Technique, Dilution Urination

Most recents protocols related to «Micelles»

Characterizing Micellar Properties via DLS

Not available on PMC !

Example 4

Dynamic light scattering (DLS) was performed on a Malvern (Westborough, MA) Zetasizer Nano instrument. The measurements were performed by diluting each fraction sample to a final concentration of 10 mg/mL in water—so as to be above the CMC for each fraction.

The micelle radius or hydrodynamic radius (R_h) was obtained using dynamic light scattering (DLS) and using a fraction concentration of 1 wt %, which is well above the CMC of all the ester fractions studied. For PS20, the R_hfor the unfractionated PS20 was about 4 nm, and the F2a and F3a fractions were about 3.9 nm. The R_hof the F1a monoester is a bit smaller, around 3.5 nm (FIG. 4A). For PS80, the micelle size was likewise a bit larger for the unfractionated PS80 sample (R_h˜4.8 nm) compared to the F2b and F3b fractions whose R_hare similar at around 4.5 nm. The R_hof the Fib, like F1a, is the smallest in the PS80 sample set, but not by much with R_h˜4.3 nm (FIG. 4B).

US11865177B2. Composition and methods for stabilizing liquid protein formulations (2024-01-09). Genentech, Inc. [US]. Inventors: Anthony Tomlinson [US], Barthelemy Luc Demeule [US], Isidro Angelo Eleazar Zarraga [US].

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Patent 2024

Esters Hydrodynamics Micelles Radius

Determining Critical Micelle Concentration of PS Fractions

Not available on PMC !

Example 2

Purified PS fractions were assessed for their critical micelle concentration (CMC) using the fluorescent dye N-Phenylnaphthalen-1-amine (NPN). This assay was performed by making 2-fold serial dilutions into a diluent composed of 0.15 M sodium chloride, 0.05 M TRIS, 5% ACN, 5 M N-phenyl-1-naphtylamine and 15 ppm Brij35 at pH 8.0. The samples were analyzed immediately in a Molecular Devices Spectramax M5 fluorescence plate reader with excitation at 350 nm and emission at 420 nm.

For PS20, the order of increasing CMC was F3a>F2a>F1a, consistent with the order of hydrophobicity. The CMC was widely separated, with ˜0.1 wt % for F1a, ˜0.015 wt % for F2a, and ˜0.001 wt % for F3a, corresponding to approximately 500 fluorescence units change from the baseline (FIG. 2A). In contrast, while the PS80 ester CMCs had similar ordering, the range of the values was much narrower, spanning just 0.001 to 0.003 wt % (FIG. 2B).

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Patent 2024

Amines Biological Assay Esters Fluorescence Fluorescent Dyes MCC protocol Medical Devices Micelles Sodium Chloride Technique, Dilution Tromethamine

Synthesis of Selenium Nanoparticles via Chemical Reduction

SeNPs were synthesized using a multisolution chemical reduction method,
in which SeO₂ was reduced by NaTP in the presence of the
particle stabilizer SDS. Initially, all glassware was washed with
a mild detergent and rinsed with deionized water. Solution I was prepared
by dissolving SDS and SeO₂ in deionized water. Solution
II was prepared by dissolving SDS and NaTP in deionized water. The
concentration of SDS in solutions I and II was chosen to be well above
its critical micelle concentration. The concentrations of SeO₂ and NaTP in solutions I and II were varied such that the
molar ratio of the selenium precursor to reducing agent was in the
range of 0.51–0.69.
Both solutions I and II were placed
into a temperature-controlled refrigeration unit held at 16 °C
while being thoroughly mixed. Once both solutions were sufficiently
mixed, solution II was promptly added to solution I to generate solution
III. Solution III was left in the refrigeration unit while mixing,
until the appearance of an orange/red color, which signified the formation
of SeNPs.
Once the SeNPs were determined to be of the desired
size, the SeNP
solutions were washed by centrifugation. Briefly, the SeNP solutions
were centrifuged until the appearance of a SeNP pellet at the base
of the centrifuge tubes. The supernatant of the washed solution was
discarded, and the SeNP pellet was resuspended using deionized water
to a volume which corresponded to an optical density of 20 ±
1. The SeNP solutions were then stored at 16 °C.

Bradley Z., Coleman P.A., Courtney M.A., Fishlock S., McGrath J., Uniacke-Lowe T., Bhalla N., McLaughlin J.A., Hogan J., Hanrahan J.P., Yan K.T, & McKee P. (2023). Effect of Selenium Nanoparticle Size on IL-6 Detection Sensitivity in a Lateral Flow Device. ACS Omega, 8(9), 8407-8414.

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Publication 2023

ARID1A protein, human Centrifugation Detergents Micelles Reducing Agents Selenium sulfoenolpyruvate

Activation of Aged Murine BMDCs

The effects of combinations of polymeric nanoparticles, micelles, and various small molecule agonists on the activation of bone marrow derived DCs (BMDCs) harvested from the femur and tibia of aged (≥20 months) C57BL/6 male mice (n = 6) were studied. Bone marrow cells were cultured as outlined in Lutz et al. [101 (link)]. Briefly, cells were cultured in 10 mL RPMI 1640 medium supplemented with 100 U/mL penicillin, 100 mg/mL streptomycin, 2 mM glutamine, 10% FBS, and 20 ng/mL granulocyte-macrophage colony-stimulating factor (GM-CSF, Cat. #FB0875711Z, Peprotech, Rocky Hill, NJ) at approximately 5 × 10⁶ cells per 100 mm plate. On day 3 of culture, 10 mL of medium containing GM-CSF was added. On days 6 and 8 of the culture period, approximately half of the total volume of medium was removed and replaced with freshly supplemented RPMI. On day 10 plates were gently rinsed to harvest non-adherent DCs for assessment of activation and costimulatory expression. Animals were obtained from Jackson Laboratory (Bar Harbor, ME) and maintained at Iowa State University following IACUC protocol #IACUC-20-199.

Ananya A., Holden K.G., Gu Z., Nettleton D., Mallapragada S.K., Wannemuehler M.J., Kohut M.L, & Narasimhan B. (2023). “Just right” combinations of adjuvants with nanoscale carriers activate aged dendritic cells without overt inflammation. Immunity & Ageing : I & A, 20, 10.

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Publication 2023

agonists Animals Bone Marrow Bone Marrow Cells Cells Femur Glutamine Granulocyte-Macrophage Colony-Stimulating Factor Institutional Animal Care and Use Committees Males Mice, Inbred C57BL Micelles Penicillins Polymers Streptomycin Tibia

Synthesis and Characterization of Pentablock Copolymer Micelles

The pentablock copolymer (PDEAEM–PEO-PPO–PEO-PDEAEM) was synthesized following our previously published protocol [46 (link)]. In short, atom transfer radical polymerization (ATRP) was used to synthesize the pentablock copolymer using a brominated Pluronic®-F127 as macroinitiator. The Pluronic F127 was dissolved in tetrahydrofuran and reacted overnight with triethylamine and 2-bromoisobutyryl. To validate the end group functionalization, the product was precipitated in n-hexane and analyzed by ¹H NMR. The macroinitiator and DEAEM monomer were then reacted by ATRP to synthesize the pentablock copolymer, with copper(I) oxide nanoparticles acting as the catalyst and N-propylpyrilidine methanamine acting as the complexing ligand [103 (link)]. The pentablock copolymer was characterized using ¹H NMR to determine purity and molecular weight (15,000 g/mol). The pentablock copolymer was dissolved in aqueous solution (12.5 μg/mL) to yield micelles.

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Publication 2023

1H NMR Copper Ligands methylamine Micelles n-hexane Oxides PEO-PPO-PEO Pluronic F-127 Polymerization tetrahydrofuran triethylamine

Top products related to «Micelles»

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Zetasizer nano zs90 by Malvern Panalytical

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The Nano ZS90 is a dynamic light scattering (DLS) instrument used for measuring the size of particles and molecules in the nanometer range. It utilizes a laser light source and a sensitive detector to analyze the Brownian motion of the particles, allowing for the determination of their hydrodynamic size.

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The Zetasizer Nano is a lab equipment product offered by Malvern Panalytical. It is a dynamic light scattering (DLS) instrument used to measure the size and size distribution of particles, molecules, and colloids in suspension or solution.

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What are the different types of micelles and how do they differ?

Micelles can exist in various forms, including spherical, cylindrical, and lamellar structures. Spherical micelles are the most common, with a hydrophilic exterior and hydrophobic interior that can solubilize and transport non-polar compounds. Cylindrical micelles have a elongated shape, while lamellar micelles form thin, sheet-like structures. The specific type of micelle that forms depends on factors like the surfactant or lipid composition, concentration, and environmental conditions.

How can micelles be used in drug delivery applications?

Micelles are particularly useful for delivering hydrophobic drugs. The hydrophobic core of the micelle can encapsulate and solubilize these drugs, while the hydrophilic exterior helps improve their bioavailability and circulation time in the body. This makes micelles an effective drug delivery system, especially for potent but poorly water-solulbe medications. Micelle-based drug formulations can also help target specific tissues or cells, improving the therapeutic efficacy and reducing side effects.

What are some common challenges in working with micelles and how can PubCompare.ai help?

One key challenge in working with micelles is ensuring reproducibility and consistency across experiments. Factors like temperature, pH, and ionic strength can impact micelle formation and behavior, making it difficult to replicate results. PubCompare.ai's AI-powered platform can help address this by allowing researchers to quickly screen and compare the most effective micelle-related protocols from literature, preprints, and patents. The platform's data-driven insights can highlight critical factors that influence micelle performance, enabling you to choose the optimal protocols for your specific research needs and enhance reproducibility.

How can PubCompare.ai assist in optimizing micelle-based research protocols?

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More about "Micelles"

Micelles are self-assembling nanostructures composed of amphiphilic molecules, such as surfactants or lipids, that form in aqueous solutions.
These tiny, spherical aggregates have a hydrophilic exterior and a hydrophobic interior, allowing them to solubilize and transport hydrophobic compounds.
Micelles play a crucial role in various biological and technological applications, including drug delivery, detergency, and nanomaterial synthesis.
Understanding the formation, structure, and properties of micelles is essential for optimizing research protocols and enhancing reproducibility in areas like micellar analysis.
Techniques like dynamic light scattering (DLS) using instruments such as the Zetasizer Nano ZS, Zetasizer Nano ZS90, and Nano ZS90 can provide valuable insights into the size, size distribution, and stability of micelles.
Flow cytometry using the FACSCalibur can also be used to analyze and characterize micelles.
Additionally, microscopy techniques like confocal laser scanning microscopy (CLSM) with the LSM 710 or transmission electron microscopy (TEM) with the HT7700 can provide visual information about micelle structure and morphology.
PubCompare.ai's AI-powered platform leverages these technologies to provide data-driven insights and help researchers locate and compare the best micelle-related protocols from literature, preprints, and patents.
This experience the future of protocol optimization and enhance reproducibility in your micelle research.