Well-ordered self-assembled monolayer surfaces can be used to enhance the growth of protein crystals

Pham, Tan Nhat; Lai, Denton; Ji, David; Tuntiwechapikul, Wirote; Friedman, Jonathan M.; Lee, T Randall

doi:10.1016/j.colsurfb.2004.01.003

Cited by 37 publications

(26 citation statements)

References 15 publications

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“…The possible explanation of this behavior is that LB template operates whether like rough surface (demonstrated by AFM images [13]) or like nucleant agent by nonspecific attraction and local interactions between charged residues of protein in solution and ionizable group on LB template surface. Another possible explanation is that, from LB template, large aggregates of protein fall in drop.…”

Section: Effects Of Lb Templatementioning

confidence: 99%

The Role of Langmuir-Blodgett (Lb) Protein Thin Film in Protein Crystal Growth by Lb Nanotemplate and Robot

Pechkova¹

2014

J Nanomed Nanotechnol

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Keywords: Classical hanging drop vapor diffusion method;Langmuir-Blodgett (LB) protein thin film; Lysozyme; Ribonuclase A; Proteinase K; Thaumatin Protein crystallography will remain the most powerfull tool for protein 3D structure investigation in the foreseeable future [1,2]. It is essential instrument enable to helping to provide new insights for drug development and for the understanding of molecular mechanisms [3].The growth of macromolecular crystals and the influence of chemical and biochemical parameters on their solubility are quite understood, but in order to gain a better and more precise understanding of the effect of physical parameters, such as temperature, magnetic, electric and gravitational fields [4], further investigations are needed.The nucleation and the growth of crystals from aqueous solutions are influenced by physical chemical variables and are altered by convective currents due to gradients caused by temperature [5] and concentration difference [6], whilst this gradient is minimal in microgravity [7]. Using LB technology is possible to improve both crystal radiation stability [8] and quality of diffraction [9].In the process of protein crystallization, nucleation is an important first step for crystal growth [10]. Several research studies have demonstrated that inorganic crystals can be used as nucleant [11]. Recent investigations have proven that inorganic materials (such as micromica and chlorite [12], complex interfaces and patterns formed by self-assembly monolayers, called SAMs, on gold [13]) can regulate nucleation because these materials can accelerate the induction of nucleation and generate larger crystals [14]. Several studies were conducted in order to investigate the effect of pH on crystal growth [15] or the mechanisms of photochemically-induced crystallization [16].Results of previous studies demonstrated that a nanostructured protein template could stimulate nucleation and crystal growth. Using this new technique, human CK2 was successfully crystallized [3] and the role of water was madee evident [17].In the present work we studied the role of LB thin film as template in order to evaluate the changes in crystal growth and the LB contribution to crystal growth at very low concentration of protein.We developed a modification of classical hanging drop vapor diffusion method ( Figure 1A) with the aim of obtaining an acceleration AbstractThe crystal growth of biological macromolecules is a very complicated process involving numerous parameters, such as pressure, pH, micro-gravity, photochemical and mechanical induction of nucleation. The utilization of Langmuir-Blodgett (LB) thin film as a template plays an important role in order to produce well-diffracting, stable and radiation-resistant protein crystals. LB nanotemplate crystallization method is a modification of the classical hanging drop vapor diffusion method. We tested four standard proteins, changing different parameters such as protein and salt concentration, number of LB layers etc., in order to verify the real role o...

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Section: Effects Of Lb Templatementioning

confidence: 99%

The Role of Langmuir-Blodgett (Lb) Protein Thin Film in Protein Crystal Growth by Lb Nanotemplate and Robot

Pechkova¹

2014

J Nanomed Nanotechnol

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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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“…[ 3 ] On the other hand, the development of suitable materials for controlled heterogeneous nucleation might facilitate biomacromolecular crystallization in a variety of experimental conditions which are not conventionally fruitful. [4][5][6] Therefore, a multiplicity of substrates, able to force molecules to come together by chemical [ 7,8 ] or physical constrains, [9][10][11][12] were investigated so far with the objective to obtain diffraction-quality crystals.…”

Section: Introductionmentioning

confidence: 99%

Tailored Hydrogel Membranes for Efficient Protein Crystallization

Profio

Polino

Nicoletta

et al. 2013

Adv Funct Materials

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Crystallization still represents the bottleneck in the process of protein structure determination at high resolution, despite high-throughput structural genomics programs requiring optimized crystallization strategies regarding crystal quality, time, success rate, reproducibility, and used protein amount. On the other hand, the development of suitable materials for controlled heterogeneous nucleation might facilitate biomacromolecular crystallization in a variety of experimental conditions which are not conventionally fruitful. Here, the possibility to fabricate hydrogel membranes displaying controlled chemical composition and nanostructure and to use them as heterogeneous supports for biomacromolecular crystallization is demonstrated. Diverse gel morphologies are obtained by controlling phase separation kinetics during gel layer formation on membrane support. These composite materials are found to increase the effi ciency of the crystallization process so that crystals with enhanced diffraction properties are produced at lower protein concentration than conventional technique, thus affording the possibility to improve current approaches to protein crystallization and to be adapted to specifi c targets.

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Well-ordered self-assembled monolayer surfaces can be used to enhance the growth of protein crystals

Cited by 37 publications

References 15 publications

The Role of Langmuir-Blodgett (Lb) Protein Thin Film in Protein Crystal Growth by Lb Nanotemplate and Robot

The Role of Langmuir-Blodgett (Lb) Protein Thin Film in Protein Crystal Growth by Lb Nanotemplate and Robot

Chiral crystallization of glutamic acid on self assembled films of cysteine

Tailored Hydrogel Membranes for Efficient Protein Crystallization

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