Protein Crystal-Mediated Biotemplating

Cohen-Hadar, Noa; Wine, Yariv; Lagziel-Simis, S.; Moscovich-Dagan, Hila; Dror, Yael; Frolow, Felix; Freeman, Amihay

doi:10.1615/jpormedia.v12.i3.20

Cited by 11 publications

(13 citation statements)

References 8 publications

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“…This permeability to a wide range of solutes has recently triggered attempts to explore the potential applications of the porosity of protein crystals as biotemplates by a controlled “filling” process for the fabrication of novel, nano‐structured composite materials. The quality of composites thus obtained will be strongly dependent upon the preservation of the initial protein crystal 3D biotemplate throughout the “filling” process, as was recently demonstrated by us (Cohen‐Hadar et al, 2006, 2009). Monitoring tools for the “filling” process and preservation of the crystalline template throughout the process were developed in our lab, including a detailed study on the elucidation of the molecular mechanism of protein crystal crosslinking by glutaraldehyde (Wine et al, 2007).…”

Section: Introductionmentioning

confidence: 77%

“…Protein crystals, routinely prepared for the elucidation of protein 3D structure by X‐ray crystallography, present a highly accurate 3D array of protein molecules. Along with the formation of this array a complementary 3D voids array of cavities and interconnecting channels filled with solution is also formed, with pattern, geometry and size depending on protein dimensions, shape and intermolecular interactions dominated by protein's surface composition (Cohen‐Hadar et al, 2006, 2009). The voids volume—the space occupied by the solvent—varies between 30% and 70% of crystal's total volume (Matthews, 1968).…”

Section: Introductionmentioning

confidence: 99%

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Re‐structuring protein crystals porosity for biotemplating by chemical modification of lysine residues

Cohen-Hadar

Lagziel-Simis

Wine

et al. 2010

Biotech & Bioengineering

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Protein crystals are routinely prepared for the elucidation of protein structure by X-ray crystallography. These crystals present an highly accurate periodical array of protein molecules with accompanying highly ordered porosity made of interconnected voids. The permeability of the porous protein crystals to a wide range of solutes has recently triggered attempts to explore their potential application as biotemplates by a controlled "filling" process for the fabrication of novel, nano-structured composite materials. Gaining control of the porosity of a given protein crystal may lead to the preparation of a series of "biotemplates" enabling different 'filler'/protein content ratios, resulting in different nanostructured composites. One way to gain such control is to produce a series of polymorphic forms of a given "parent-protein" crystal. As protein packing throughout crystallization is primarily dominated by the chemical composition of the surface of protein molecules and its impact on protein-protein interactions, modification of residues exposed on the surface will affect protein packing, leading to modified porosity. Here we propose to provide influence on the porosity of protein crystals for biotemplating by pre-crystallization chemical modification of lysine residues exposed on protein's surface. The feasibility of this approach was demonstrated by the serial application of chemical "modifiers" leading to protein derivatives exhibiting altered porosity by affecting protein "packing" throughout protein crystallization. Screening of a series of modifying agents for lysine modification of hen egg white lysozyme revealed that pre-crystallization modification preserving their positive charge did not affect crystal porosity, while modification resulting in their conversion to negatively charged groups induced dramatic change in protein crystal's packing and porosity. Furthermore, we demonstrate that chemical modification of lysine residues affecting modified protein packing may be simultaneously performed with the crystallization process: aldehydes generating Schiff base formation with protein's lysine residues readily affected modified protein packing, resulting in altered porosity. Our results demonstrate the feasibility of the use of site directed chemical modifications for the generation of a series of protein crystal exhibiting different porosities for biotemplating, all derived from one "parent" protein.

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Section: Introductionmentioning

confidence: 77%

Section: Introductionmentioning

confidence: 99%

Re‐structuring protein crystals porosity for biotemplating by chemical modification of lysine residues

Cohen-Hadar

Lagziel-Simis

Wine

et al. 2010

Biotech & Bioengineering

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“…Corresponding to the ordered array of molecules, the resultant interconnected holes can accommodate small molecules. 95 Additionally, throughout the crystallization process, Wine et al 96 investigated the inuence of site specic mutations of lysine residues located in the protein crystal on crystal porosity and their application as bio-templates. Based on these properties, the application of CLPCs in organic synthesis 62 and size exclusion chromatography 53 has already been developed and improved.…”

Section: Applications Of Clpcsmentioning

confidence: 99%

Cross-linked protein crystals by glutaraldehyde and their applications

et al. 2015

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Cross-linked protein crystal technology, as either a protein stabilisation or enzyme immobilisation method, has garnered more attention recently. This method not only can retain the original activity of the protein molecule but can also significantly enhance the crystals' mechanical and chemical stability. This review presents the preparation and mechanism of cross-linked protein crystals using glutaraldehyde. The mechanical, chemical and thermal properties of the cross-linked protein crystals are also reviewed in detail. In addition, this paper summarises the applications of cross-linked protein crystals in the fields of materials science, biosensors, chromatographic analysis, oral delivery and protein crystal quality improvement. Finally, the limitations and perspectives on cross-linked protein crystals are presented.Crystallisation is a well-known approach to obtain highly puri-ed proteins. During crystallisation, protein molecules can be Fig. 2 A schematic diagram of the polymerisation of glutaraldehyde. 21This journal is

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“…Protein crystals, routinely prepared for the elucidation of protein 3D structure by X-ray crystallography, present a highly accurate 3D array of protein molecules. Along with the formation of this array; a complementary 3D array of cavities is also formed, with pattern, geometry and size depending on protein dimensions, shape and intermolecular interactions (Cohen-Hadar et al, 2009). These cavity arrays-which may occupy one to two thirds of the crystal volume-are made of interconnected voids exhibiting highly ordered porosity.…”

Section: Introductionmentioning

confidence: 99%

“…The permeability of protein crystals to a wide range of solutes, may allow their ''filling'' and use as biotemplates for the fabrication of novel, nano-structured composite materials. The quality of composites thus obtained-in terms of stability and high periodicity-will be strongly dependent upon the accurate preservation of the initial protein crystal 3D template throughout the ''filling'' process, as was recently demonstrated for crosslinked crystals , 2009. Monitoring tools for the preservation and verification of the crystalline template throughout the ''filling'' process were recently developed, followed by a detailed study on the molecular mechanism of protein crystal crosslinking by glutaraldehyde (Wine et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Modification of protein crystal packing by systematic mutations of surface residues: Implications on biotemplating and crystal porosity

Wine

Cohen-Hadar

Lamed

et al. 2009

Biotech & Bioengineering

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Bioinspired nano-scale biotemplating for the development of novel composite materials has recently culminated in several demonstrations of nano-structured hybrid materials. Protein crystals, routinely prepared for the elucidation of protein 3D structures by X-ray crystallography, present an ordered and highly accurate 3D array of protein molecules. Inherent to the 3D arrangement of the protein "building blocks" in the crystal, a complementary 3D array of interconnected cavities--voids array, exhibiting highly ordered porosity is formed. The porous arrays of protein crystal may serve as a nano-structured, accurate biotemplate by a "filling" process. These cavities arrays are shaped by the mode of protein packing throughout the crystallization process. Here we propose and demonstrate feasibility of targeting site specific mutations to modify protein's surface to affect protein crystal packing, enabling the generation of a series of protein crystal "biotemplates" all originating from same parent protein. The selection of these modification sites was based on in silico analysis of protein-protein interface contact areas in the parent crystal. The model protein selected for this study was the N-terminal type II cohesin from the cellulosomal scaffold in ScaB subunit of Acetivibrio cellulolyticus and mutations were focused on lysine residues involved in protein packing as prime target. The impact of systematically mutating these lysine residues on protein packing and its resulting interconnected cavities array were found to be most significant when surface lysine residues were substituted to tryptophan residues. Our results demonstrate the feasibility of using pre-designed site directed mutations for the generation of a series of protein crystal biotemplates from a "parent" protein.

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Protein Crystal-Mediated Biotemplating

Cited by 11 publications

References 8 publications

Re‐structuring protein crystals porosity for biotemplating by chemical modification of lysine residues

Re‐structuring protein crystals porosity for biotemplating by chemical modification of lysine residues

Cross-linked protein crystals by glutaraldehyde and their applications

Modification of protein crystal packing by systematic mutations of surface residues: Implications on biotemplating and crystal porosity

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