Nanometer to Millimeter Scale Peptide-porphyrin Materials

Overview

Journal Biomacromolecules

Publisher American Chemical Society

Specialties Biochemistry
Biology
Molecular Biology

Date 2010 Sep 1

PMID 20804210

Citations 5

Authors

Daniil V Zaytsev

Fei Xie

Madhumita Mukherjee

Alexey Bludin

Borries Demeler

Robert M Breece

David L Tierney

Michael Y Ogawa

Affiliations

Soon will be listed here.

Abstract

AQ-Pal14 is a 30-residue polypeptide that was designed to form an α-helical coiled coil that contains a metal-binding 4-pyridylalanine residue on its solvent-exposed surface. However, characterization of this peptide shows that it exists as a three-stranded coiled coil, not a two-stranded one as predicted from its design. Reaction with cobalt(III) protoporphyrin IX (Co-PPIX) produces a six-coordinate Co-PPIX(AQ-Pal14)(2) species that creates two coiled-coil oligomerization domains coordinated to opposite faces of the porphyrin ring. It is found that this species undergoes a buffer-dependent self-assembly process: nanometer-scale globular materials were formed when these components were reacted in unbuffered H(2)O, while millimeter-scale, rod-like materials were prepared when the reaction was performed in phosphate buffer (20 mM, pH 7). It is suggested that assembly of the globular material is dictated by the conformational properties of the coiled-coil forming AQ-Pal14 peptide, whereas that of the rod-like material involves interactions between Co-PPIX and phosphate ion.

Citing Articles

Peptide-Tetrapyrrole Supramolecular Self-Assemblies: State of the Art.

Dognini P, Coxon C, Alves W, Giuntini F Molecules. 2021; 26(3).

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Porphyrin-Induced Protein Oxidation and Aggregation as a Mechanism of Porphyria-Associated Cell Injury.

Maitra D, Bragazzi Cunha J, Elenbaas J, Bonkovsky H, Shavit J, Omary M Cell Mol Gastroenterol Hepatol. 2019; 8(4):535-548.

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Oxygen and Conformation Dependent Protein Oxidation and Aggregation by Porphyrins in Hepatocytes and Light-Exposed Cells.

Maitra D, Carter E, Richardson R, Rittie L, Basrur V, Zhang H Cell Mol Gastroenterol Hepatol. 2019; 8(4):659-682.e1.

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The Structure and Topology of α-Helical Coiled Coils.

Lupas A, Bassler J, Dunin-Horkawicz S Subcell Biochem. 2017; 82:95-129.

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Solvent-Tuned Self-Assembled Nanostructures of Chiral l/d-Phenylalanine Derivatives of Protoporphyrin IX.

Bobe M, Al Kobaisi M, Bhosale S, Bhosale S ChemistryOpen. 2015; 4(4):516-22.

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References

Bromley E, Channon K, Moutevelis E, Woolfson D . Peptide and protein building blocks for synthetic biology: from programming biomolecules to self-organized biomolecular systems. ACS Chem Biol. 2008; 3(1):38-50. DOI: 10.1021/cb700249v. View

Su J, Hodges R, Kay C . Effect of chain length on the formation and stability of synthetic alpha-helical coiled coils. Biochemistry. 1994; 33(51):15501-10. DOI: 10.1021/bi00255a032. View

Hong J, Kharenko O, Ogawa M . Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up. Inorg Chem. 2006; 45(25):9974-84. PMC: 2566827. DOI: 10.1021/ic060222j. View

Pelton J, McLean L . Spectroscopic methods for analysis of protein secondary structure. Anal Biochem. 2000; 277(2):167-76. DOI: 10.1006/abio.1999.4320. View

Woodruff W, Adams D, Spiro T, Yonetani T . Resonance Raman spectra of cobalt myoglobins and cobalt porphyrins. Evaluation of protein effects on porphyrin structure. J Am Chem Soc. 1975; 97(7):1695-8. DOI: 10.1021/ja00840a012. View

Horcas I, Fernandez R, Gomez-Rodriguez J, Colchero J, Gomez-Herrero J, Baro A . WSXM: a software for scanning probe microscopy and a tool for nanotechnology. Rev Sci Instrum. 2007; 78(1):013705. DOI: 10.1063/1.2432410. View

Zahran Z, Chooback L, Copeland D, West A, Richter-Addo G . Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations. J Inorg Biochem. 2007; 102(2):216-33. PMC: 2771112. DOI: 10.1016/j.jinorgbio.2007.08.002. View

McAllister K, Zou H, Cochran F, Bender G, Senes A, Fry H . Using alpha-helical coiled-coils to design nanostructured metalloporphyrin arrays. J Am Chem Soc. 2008; 130(36):11921-7. PMC: 3663296. DOI: 10.1021/ja800697g. View

Tsurkan M, Ogawa M . Formation of peptide nanospheres and nanofibrils by metal coordination. Biomacromolecules. 2007; 8(12):3908-13. DOI: 10.1021/bm700879t. View

10.

Dublin S, Conticello V . Design of a selective metal ion switch for self-assembly of peptide-based fibrils. J Am Chem Soc. 2007; 130(1):49-51. DOI: 10.1021/ja0775016. View

11.

Wagschal K, Tripet B, Lavigne P, Mant C, Hodges R . The role of position a in determining the stability and oligomerization state of alpha-helical coiled coils: 20 amino acid stability coefficients in the hydrophobic core of proteins. Protein Sci. 1999; 8(11):2312-29. PMC: 2144206. DOI: 10.1110/ps.8.11.2312. View

12.

Woolfson D, Ryadnov M . Peptide-based fibrous biomaterials: Some things old, new and borrowed. Curr Opin Chem Biol. 2006; 10(6):559-67. DOI: 10.1016/j.cbpa.2006.09.019. View

13.

Kharenko O, Ogawa M . Metal-induced folding of a designed metalloprotein. J Inorg Biochem. 2004; 98(11):1971-4. DOI: 10.1016/j.jinorgbio.2004.07.015. View

14.

Ellis-Behnke R, Liang Y, You S, Tay D, Zhang S, So K . Nano neuro knitting: peptide nanofiber scaffold for brain repair and axon regeneration with functional return of vision. Proc Natl Acad Sci U S A. 2006; 103(13):5054-9. PMC: 1405623. DOI: 10.1073/pnas.0600559103. View

15.

Lauher J, Ibers J . Stereochemistry of cobalt porphyrins. II. The characterization and structure of meso-tetraphenylporphinatobis(imidazole)cobalt(3) acetate monohydrate monochloroformate,(Co(Im)2(TPP))(OAc)-H2O-CHCl3. J Am Chem Soc. 1974; 96(14):4447-52. DOI: 10.1021/ja00821a017. View

16.

Harbury P, Zhang T, Kim P, Alber T . A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science. 1993; 262(5138):1401-7. DOI: 10.1126/science.8248779. View

17.

Tsurkan M, Ogawa M . Metal-mediated peptide assembly: use of metal coordination to change the oligomerization state of an alpha-helical coiled-coil. Inorg Chem. 2007; 46(17):6849-51. DOI: 10.1021/ic700958h. View

18.

Woodruff W, Spiro T, Yonetani T . Resonance Raman spectra of cobalt-substituted hemoglobin: cooperativity and displacement of the cobalt atom upon oxygenation. Proc Natl Acad Sci U S A. 1974; 71(4):1065-9. PMC: 388163. DOI: 10.1073/pnas.71.4.1065. View

19.

Gazit E . Self-assembled peptide nanostructures: the design of molecular building blocks and their technological utilization. Chem Soc Rev. 2007; 36(8):1263-9. DOI: 10.1039/b605536m. View

20.

Kerman K, Kraatz H . Metals coordinate protein-protein interactions. Angew Chem Int Ed Engl. 2008; 47(35):6522-4. DOI: 10.1002/anie.200801169. View