PATIC: a conformationally constrained photoisomerizable amino acid

Zhang, J.; James, Daniel F. V.; Woolley, G. Andrew

doi:10.1034/j.1399-3011.1999.00061.x

Cited by 7 publications

(3 citation statements)

References 43 publications

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“…Compounds that undergo larger dipole moment changes upon photoisomerization such as spiropyran/merocyanine-based compounds could be substituted for azobenzene in the channel. Strategies for increasing the effects of photoisomerization on channel conductance might also include the use of conformationally restrained azobenzene analogues to control the orientation of the side-chain dipoles …”

Section: Discussionmentioning

confidence: 99%

Optical Switching of Ion−Dipole Interactions in a Gramicidin Channel Analogue

et al. 2000

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Optical control of ion channel gating could permit the functional manipulation of excitable cells. We wished to examine the feasibility of using optical switching of ion−dipole interactions as a means of switching ion flux in channels. We prepared an analogue of the ion channel gramicidin A in which an azobenzene side chain was substituted for a valine side chain at position 1. The dipole moment of the azobenzene group can be reversibly switched between approximately 3 and 0 D by cis−trans photoisomerization. The observed conductance properties of the modified channels can be understood in terms of (switchable) ion−dipole interactions that control the height of the central barrier for Cs+ and Na+ movement through the pore. The predictable behavior of the system implies that larger dipole changes or changes closer to the central axis of the pore might effect complete gating.

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Section: Discussionmentioning

confidence: 99%

Optical Switching of Ion−Dipole Interactions in a Gramicidin Channel Analogue

et al. 2000

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“…The potential for additional applications, combined with the limited number of available building blocks, has spurred the design and synthesis of new ones. We introduced phosphonic acid-bearing azobenzene-based amino acids, 33 Woolley and co-workers introduced a conformationally constrained azobenzene-based amino acid, 34 and Juodaityte and Sewald introduced two interesting azo-linked dimers of phenylalanine and O-methyltyrosine. 35 Additional amino acids based on alternative chromophores, such as the hemithioindigo, are also being developed rapidly.…”

Section: Introductionmentioning

confidence: 99%

Abc Amino Acids: Design, Synthesis, and Properties of New Photoelastic Amino Acids

Standaert

Park

2006

J. Org. Chem.

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Photoisomerizable amino acids provide a direct avenue to the experimental manipulation of bioactive polypeptides, potentially allowing real-time, remote control of biological systems and enabling useful applications in nanobiotechnology. Herein, we report a new class of photoisomerizable amino acids intended to cause pronounced expansion and contraction in the polypeptide backbone, i.e., to be photoelastic. These compounds, termed Abc amino acids, employ a photoisomerizable azobiphenyl chromophore to control the relative disposition of aminomethyl and carboxyl substituents. Molecular modeling of nine Abc isomers led to the identification of one with particularly attractive properties, including the ability to induce contractions up to 13 A in the backbone upon trans --> cis photoisomerization. This isomer, designated mpAbc, has substituents at meta and para positions on the inner (azo-linked) and outer rings, respectively. An efficient synthesis of Fmoc-protected mpAbc was executed in which the biaryl components were formed via Suzuki couplings and the azo linkage was formed via amine/nitroso condensation; protected forms of three other Abc isomers were prepared similarly. An undecapeptide incorporating mpAbc was synthesized by conventional solid-phase methods and displayed characteristic azobenzene photochemical behavior with optimal conversion to the cis isomer at 360 nm and a thermal cis --> trans half-life of 100 min at 80 degrees C.

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“…groups directly into the backbone of cyclic peptides [8-11] and have studied the conformational effects of Results and Discussion photoisomerization in these systems. Conformational effects of azobenzene-containing side chains have also Peptide Design been studied [12][13][14][15][16].…”

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confidence: 99%

Using an Azobenzene Cross-Linker to Either Increase or Decrease Peptide Helix Content upon Trans-to-Cis Photoisomerization

Flint

Kumita

Smart

et al. 2002

Chemistry & Biology

162

191

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Reversible photocontrol of peptide and protein conformation could prove to be a powerful tool for probing function in diverse biological systems. Here, we report reversible photoswitching of the helix content in short peptides containing an azobenzene cross-linker between cysteine residues at positions i, i + 4, or i, i + 11 in the sequence. Trans-to-cis photoisomerization significantly increases the helix content in the i, i + 4 case and significantly decreases the helix content in the i, i + 11 case. These cross-linker designs significantly expand the possibilities for photocontrol of peptide and protein structure.

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PATIC: a conformationally constrained photoisomerizable amino acid

Cited by 7 publications

References 43 publications

Optical Switching of Ion−Dipole Interactions in a Gramicidin Channel Analogue

Optical Switching of Ion−Dipole Interactions in a Gramicidin Channel Analogue

Abc Amino Acids: Design, Synthesis, and Properties of New Photoelastic Amino Acids

Using an Azobenzene Cross-Linker to Either Increase or Decrease Peptide Helix Content upon Trans-to-Cis Photoisomerization

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