Incorporation of artificial receptors into a protein/peptide surface: A strategy for on/off type of switching of semisynthetic enzymes

Hamachi, Itaru; Watanabe, Jun; Eboshi, Ryoji; Hiraoka, Takashi; Shinkai, Seiji

doi:10.1002/1097-0282(2000)55:6<459::aid-bip1021>3.0.co;2-r

Cited by 15 publications

(10 citation statements)

References 36 publications

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“…However, examples of the combination of thermoresponsive polymers with other globular or colloidal biomolecules and studies of their temperature‐induced coassembly have been limited 10. The wealth of studies has mainly focused on thermoresponsive polymers covalently bound to the surface of synthetic particles or individual proteins 11. For example, thermoresponsive polymers grafted covalently onto protein surfaces have yielded thermal switching of enzyme activity,12 size dependent binding,13 and self‐assembly to form spherical structures at elevated temperatures 14…”

Section: Introductionmentioning

confidence: 99%

Temperature‐Switchable Assembly of Supramolecular Virus–Polymer Complexes

Kostiainen

Pietsch

Hoogenboom

et al. 2011

Adv Funct Materials

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Here a method is presented for the temperature‐switchable assembly of viral particles into large hierarchical complexes. Dual‐functional diblock copolymers consisting of poly(diethyleneglycol methyl ether methacrylate) (poly(DEGMA)) and poly((2‐dimethylamino)ethyl methacrylate) (poly(DMAEMA)) blocks self‐assemble electrostatically with cowpea chlorotic mottle virus (CCMV) particles into micrometer‐sized objects as a function of temperature. The poly(DMAEMA) block carries a positive charge, which can interact electrostatically with the negatively charged outer surface of the CCMV capsid. When the solution temperature is increased above 40 °C, to cross the cloud point temperature (Tcp) of the DEGMA block, the polymer chains collapse on the surface of the virus particle, which makes them partially hydrophobic, and consequently causes the formation of large hierarchical assemblies. Disassembly of the virus–polymer complexes can be induced by reducing the solution temperature below the Tcp, which allows the poly(DEGMA) blocks to rehydrate and free virus particles to be released. The assembly process is fully reversible and can sustain several heating–cooling cycles. Importantly, this method relies on reversible supramolecular interactions and therefore avoids the irreversible covalent modification of the particle surface. This study illustrates the potential of temperature‐responsive polymers for controlled binding and releasing of virus particles.

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Section: Introductionmentioning

confidence: 99%

Temperature‐Switchable Assembly of Supramolecular Virus–Polymer Complexes

Kostiainen

Pietsch

Hoogenboom

et al. 2011

Adv Funct Materials

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“…Building blocks for the coordination of metal ions and their incorporation into peptides or proteins have already been described 12–18. However, in most cases several amino acids are necessary to form stable metal complexes.…”

Section: Resultsmentioning

confidence: 99%

Metal‐Chelating Amino Acids As Building Blocks For Synthetic Receptors Sensing Metal Ions And Histidine‐Tagged Proteins

et al. 2003

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Protein structure and function rely on a still not fully understood interplay of energetic and entropic constraints defined by the permutation of the twenty genetically encoded amino acids. Many attempts have been undertaken to design peptide-peptide interaction pairs and synthetic receptors de novo by using this limited number of building blocks. We describe a rational approach to creating a building block based on a tailored metal-chelating amino acid. Nepsilon,Nepsilon-bis(carboxymethyl)-L-lysine can be flexibly introduced into peptides by 9-fluorenylmethoxycarbonyl solid-phase chemistry. The corresponding metal-chelating peptides act as metal sensors and synthetic receptors for histidine-tagged proteins. These biochemical tweezers will open new ways to control protein-protein interactions, to design peptide-based interaction pairs, or to generate switchable protein function.

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“…The synthesis of Fmoc-Lys(IDA)-OH has been previously described [19]. The preparation of peptides containing the IDA moiety was carried out according to the previously described procedure [15] using Fmoc-Lys(IDA(OtBu))-OH as the building block. HBTU and DIPEA (TCI America, Portland, OR) in N,N -dimethylformamide (DMF) (VWR, West Chester, PA) were used as coupling and activating reagents, respectively.…”

Section: 0 Materials and Methodsmentioning

confidence: 99%

“…Metal-chelating groups have been used in the areas of protein purifications [12,13], peptide/protein engineering [14,15], and designing of nucleic acid probes targeting specific DNA molecules [16]. …”

Section: 0 Introductionmentioning

confidence: 99%

Synthesis and evaluation of phosphopeptides containing iminodiacetate groups as binding ligands of the Src SH2 domain

Schuler

Ahmadibeni

et al. 2009

Bioorganic Chemistry

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Phosphopeptide pTyr-Glu-Glu-Ile (pYEEI) has been introduced as an optimal Src SH2 domain ligand. Peptides, Ac-K(IDA)pYEEIEK(IDA) (1), Ac-KpYEEIEK (2), Ac-K(IDA)pYEEIEK (3), and Ac-KpYEEIEK(IDA) (4), containing 0-2 iminodiacetate (IDA) groups at the N-and C-terminal lysine residues were synthesized and evaluated as the Src SH2 domain binding ligands. Fluorescence polarization assays showed that peptide 1 had a higher binding affinity (K d = 0.6 µM) to the Src SH2 domain when compared with Ac-pYEEI (K d = 1.7 µM), an optimal Src SH2 domain ligand, and peptides 2−4 (K d = 2.9-52.7 µM). The binding affinity of peptide 1 to the SH2 domain was reduced by more than two fold (K d = 1.6 µM) upon addition of Ni 2+ (300 µM), possibly due to modest structural effect of Ni 2+ on the protein as shown by circular dichroism experimental results. The binding affinity of 1 was restored in the presence of EDTA (300 µM) (K d = 0.79 µM). These studies suggest that peptides containing IDA groups may be used for designing novel SH2 domain binding ligands. Keywordsphosphopeptides; metal chelation; iminodiacetate group; SH2 domain; UV titration; fluorescence polarization; circular dichroism IntroductionSrc, one of the first studied non-receptor tyrosine kinases, has been implicated in the genesis and progression of multiple types of human diseases including colon, breast, lung cancers, osteoporosis, and inflammation-mediated bone loss [1,2]. Src tyrosine kinase contains three major domains, in the order from N-to C-terminal, two regulatory Src homology (SH) domains (SH3 and SH2 domains), and a kinase domain. The Src SH2 domain is a relatively small protein module of approximately 100 amino acids and has extraordinary ability to recognize specifically sequences containing phosphotyrosine residue (pTyr), thereby facilitating phosphorylation-dependent protein-protein interactions that result in signal transduction process [3]. Short peptide inhibitors capable of disrupting these interactions have been designed as useful tools in the mechanistic studies of the Src SH2 domain interactions and as potential NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscript inhibitors for further pharmaceutical development [4−8]. The Src SH2 domain preferentially binds peptides with the sequence pTyr-Glu-Glu-Ile (pYEEI) with high affinity [9].The use of conformationally constrained peptides has been shown to be an effective strategy in developing therapeutic peptidic and peptidomimetic agents [10,11]. Constrained peptides are usually more stable towards enzymatic degradations. We previously reported the synthesis and evaluation of a series of covalently bonded conformationally constrained peptide analogues based on the optimal sequence pYEEI as inhibitors of the Src SH2 domain [8]. A number of conformationally constrained peptides showed at least 100-fold fold increase in the binding affinities to the Src SH2 domain relative to pYEEI and the corresponding linear peptides, respectively. The enhancement in binding affinities was a...

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Incorporation of artificial receptors into a protein/peptide surface: A strategy for on/off type of switching of semisynthetic enzymes

Cited by 15 publications

References 36 publications

Temperature‐Switchable Assembly of Supramolecular Virus–Polymer Complexes

Temperature‐Switchable Assembly of Supramolecular Virus–Polymer Complexes

Metal‐Chelating Amino Acids As Building Blocks For Synthetic Receptors Sensing Metal Ions And Histidine‐Tagged Proteins

Synthesis and evaluation of phosphopeptides containing iminodiacetate groups as binding ligands of the Src SH2 domain

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