Improved protein crystallization by vapor diffusion from drops in contact with transparent, self-assembled monolayers on gold-coated glass coverslips

Ji, David; Arnold, Christine; Graupe, Michael; Beadle, Eric; Dunn, Robert V; Phan, My N; Villazana, Ramon J.; Benson, R. E.; Colorado, Ramon; Lee, T Randall; Friedman, Jonathan M.

doi:10.1016/s0022-0248(00)00541-8

Cited by 19 publications

(11 citation statements)

References 13 publications

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“…Self-assembled monolayers terminated in (EG) 3 OH were prepared by sputter-coating cleaned glass coverslips with a transparent gold layer (25 Å chromium and 150 Å gold) using a CMS-18 Multi Target Sputter Deposition machine (Kurt Lesker, Clairton, PA) [44], and immersing them overnight in 1 mM solution of 1-mercapto-11-undecyl tri(ethylene glycol) (Asemblon Inc., Redmond, WA) prepared in 99.9% methanol (Sigma-Aldrich, Saint Louis, MO) according to [41].…”

Section: Methodsmentioning

confidence: 99%

Quantifying the Performance of Protein‐Resisting Surfaces at Ultra‐Low Protein Coverages using Kinesin Motor Proteins as Probes

Katira¹,

Agarwal²,

Fischer³

et al. 2007

Advanced Materials

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Surfaces resistant to protein adsorption are very desirable for a variety of applications in biomedical engineering and bionanotechnology, since protein adsorption is often the first step in a cascade of events leading to systems failure. Initial efforts to create adsorption-resistant surfaces succeeded in reducing the adsorption by 80% compared to untreated surfaces to 100 ng cm -2 by employing poly(ethylene glycol) coatings.[1]Recently, optimization of brush density and morphology has reduced adsorption to 1 ng cm -2 or less.[2] These coverages, equal to about one tenth of a percent of a monolayer, represent the detection limit for several characterization techniques, including SPR [2,3] and radiolabeling.[4] However, biological effects can be observed for protein coverages below this detection limit. For example, adsorption of blood proteins can initiate the intrinsic coagulation cascade at low coverage.[5] Therefore more sensitive techniques for the measurement of protein adsorption are needed. Moreover, if protein adsorption is exceedingly slow, higher sensitivity would permit an accelerated quantification of the performance of the surface (e.g. within hours instead of days). Non-fouling surfaces are also a critical part of hybrid nanodevices, which utilize precisely positioned biomolecules in an artificial environment.[6] For example, controlled adsorption of kinesin, [7][8][9][10][11][12][13][14] myosin, [15][16][17] and F1-ATPase motors [18] has been utilized for the design of molecular shuttles and nanopropellers. Adsorption of motor proteins outside the intended regions at densities down to one motor per square micrometer (0.04 ng cm -2) can lead to loss of device function, since individual motors can already bind and transport the associated filaments outside their intended tracks.The binding of associated filaments, such as microtubules or actin filaments, is readily observed by fluorescence microscopy, since these filaments are composed of thousands of protein subunits and carry typically at least a thousand covalently linked fluorophores. [19,20] Howard et al. demonstrated in 1989 that observing the attachment of microtubules from solution to surface-adhered kinesin motors enables the determination of motor densities as low as 2 proteins per lm 2 by measuring the rate of microtubule attachment. [21,22] Attachment rate measurements have subsequently been adapted to the determination of relative kinesin motor activity on different surfaces [9] and to the evaluation of guiding structures for microtubule transport [10,23] Since kinesins long tail domain evolved to efficiently connect to cargo, we hypothesize that it can serve as a particularly efficient probe for attachment points on the surface. [24,25] . Landing rate measurements enable the measurement of absolute coverages of functional kinesins in the range of 0.004 -1 ng cm -2 , thus enabling to differentiate the performance of even the best non-fouling surfaces. While landing rate measurements in effect count individual proteins, their complexity ...

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Section: Methodsmentioning

confidence: 99%

Quantifying the Performance of Protein‐Resisting Surfaces at Ultra‐Low Protein Coverages using Kinesin Motor Proteins as Probes

Katira¹,

Agarwal²,

Fischer³

et al. 2007

Advanced Materials

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“…14,15 Chiral surfaces based on self-assembled monolayers (SAM) and Langmuir-Blodgett 16 films have been used for many years to study the influence of well-defined functionalized surfaces on nucleation, polymorphism, and selective orientation of crystals. For instance, crystals of many different materials have been grown on SAM, including proteins, 17,18 enantiomerically pure amino acids, [19][20][21] semiconductors, 22 and biominerals. [23][24][25] SAMs have also been employed to control crystal morphology and orientation, for example Swift and coworkers described that SAMs can be used to direct the nucleation and subsequent orientation of crystals 26,27 and to control crystal polymorphism.…”

Section: Introductionmentioning

confidence: 99%

Chiral crystallization of glutamic acid on self assembled films of cysteine

Dressler

Mastai

2007

Chirality

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In this article, we describe the preparation and use of chiral surfaces derived from enantiomerically pure crystals of amino acids. For this purpose, we chose to employ a self-assembly process to grow nanoscale chiral films of (+)-L or (-)-D cysteine, onto gold surfaces. We utilized those chiral films as resolving auxiliaries in the crystallization of enantiomers from solutions. To demonstrate the chiral discriminating ability of the chiral surfaces in crystallization processes, we investigated the crystallization of rac-glutamic acid onto the chiral films. Our study demonstrates the potential application of chiral films to control chirality throughout crystallization, where one enantiomer crystallizes on the chiral surfaces with relatively high enantiomeric excess. In addition, crystallization of pure glutamic acid enantiomers, and its racemic compound on to chiral films resulted in crystal morphology modification with preferred crystal orientation, which assists in the interpretation of the ability of our chiral surfaces to function as chiral selectors.

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“… 15 Many applications of SAMs in biotechnology, 16 bio-sensoring, 17 organic electronics, 18 and photonics 19 have been reported. With regard to crystallization, the self-assembly of selected building blocks in monolayers or multilayers has been adopted to create supports for polymorph selection 20 and protein crystallization, 21 as well as for oriented growth 22 and nucleation kinetics. 23 For example, SAMs were patterned to create hydrophobic and hydrophilic areas to force the crystallization of glycine at the nanoscale 24 or even coupled to porous layers, such as metal–organic frameworks, for crystal engineering.…”

Section: Introductionmentioning

confidence: 99%

Role of Self-Assembled Surface Functionalization on Nucleation Kinetics and Oriented Crystallization of a Small-Molecule Drug: Batch and Thin-Film Growth of Aspirin as a Case Study

Artusio

Fumagalli

Valsesia

et al. 2021

ACS Appl. Mater. Interfaces

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The present paper assesses the heterogeneous nucleation of a small-molecule drug and its relationship with the surface chemistry of engineered heteronucleants. The nucleation of aspirin (ASA) was tuned by different functional groups exposed by self-assembled monolayers (SAMs) immobilized on glass surfaces. Smooth topographies and defect-free surface modification allowed the deconvolution of chemical and topographical effects on nucleation. The nucleation induction time of ASA in batch crystallization was mostly enhanced by methacrylate and amino groups, whereas it was repressed by thiol groups. In this perspective, we also present a novel strategy for the evaluation of surface–drug interactions by confining drug crystallization to thin films and studying the preferential growth of crystal planes on different surfaces. Crystallization by spin coating improved the study of oriented crystallization, enabling reproducible sample preparation, minimal amounts of drug required, and short processing time. Overall, the acid surface tension of SAMs dictated the nucleation kinetics and the extent of relative growth of the ASA crystal planes. Moreover, the face-selective action of monolayers was investigated by force spectroscopy and attributed to the preferential interaction of exposed groups with the (100) crystal plane of ASA.

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Improved protein crystallization by vapor diffusion from drops in contact with transparent, self-assembled monolayers on gold-coated glass coverslips

Cited by 19 publications

References 13 publications

Quantifying the Performance of Protein‐Resisting Surfaces at Ultra‐Low Protein Coverages using Kinesin Motor Proteins as Probes

Quantifying the Performance of Protein‐Resisting Surfaces at Ultra‐Low Protein Coverages using Kinesin Motor Proteins as Probes

Chiral crystallization of glutamic acid on self assembled films of cysteine

Role of Self-Assembled Surface Functionalization on Nucleation Kinetics and Oriented Crystallization of a Small-Molecule Drug: Batch and Thin-Film Growth of Aspirin as a Case Study

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