α,β-Dehydro-Dopa: A Hidden Participant in Mussel Adhesion

Biochemistry

Volumn 55, Issue 5, 2016, Pages 743-750

  Mirshafian, Razieh ^a   Wei, Wei ^a   Israelachvili, Jacob N ^b   Waite, J Herbert ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b University of California   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADHESION; ALKALINITY; MOLLUSCS; OXIDATION; PROTEINS; ULTRAVIOLET VISIBLE SPECTROSCOPY;

ADSORPTION CAPACITIES; CHEMICAL ENVIRONMENT; CHEMICAL SIGNATURES; L-3 ,4-DIHYDROXYPHENYLALANINE; MUSSEL ADHESIVE PROTEINS; OXIDATION PRODUCTS; PROTEIN SECONDARY STRUCTURE; UV-VIS SPECTROSCOPY;

CYCLIC VOLTAMMETRY;

ALPHA,BETA DEHYDRO DOPA; DOPA; ESTER; MUSSEL ADHESIVE PROTEIN; N ACETYL ALPH,BETA DEHYDRO DOPA ETHYL ESTER; N ACETYL ALPHA,BETA DEHYDRO DOPA ETHYL ESTER; N ACETYL ALPHA,BETA DOPA QUINONE ETHYL ESTER; PEPTIDYL DOPA; QUINONE DERIVATIVE; UNCLASSIFIED DRUG; ADHESIVE PROTEIN, MUSSEL; PROTEIN;

ADSORPTION; ALKALINITY; ARTICLE; BETA SHEET; CHEMICAL ENVIRONMENT; CROSS LINKING; CYCLIC POTENTIOMETRY; MUSSEL; OXIDATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; QUARTZ CRYSTAL MICROBALANCE; TAUTOMER; ULTRAVIOLET SPECTROSCOPY; ANALOGS AND DERIVATIVES; ANIMAL; BIVALVE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; INFRARED SPECTROSCOPY; OXIDATION REDUCTION REACTION; PHYSIOLOGY; POLYMERIZATION; ULTRAVIOLET SPECTROPHOTOMETRY;

ANIMALS; BIVALVIA; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DIHYDROXYPHENYLALANINE; OXIDATION-REDUCTION; POLYMERIZATION; PROTEINS; QUARTZ CRYSTAL MICROBALANCE TECHNIQUES; SPECTROPHOTOMETRY, ULTRAVIOLET; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 84957889137     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b01177     Document Type: Article

References (31)

1. Bandara, N., Zeng, H., and Wu, J. (2013) Marine mussel adhesion: biochemistry, mechanisms, and biomimetics J. Adhes. Sci. Technol. 27, 2139-2162 10.1080/01694243.2012.697703
2. Lee, B. P., Messersmith, P. B., Israelachvili, J. N., and Waite, J. H. (2011) Mussel-inspired adhesives and coatings Annu. Rev. Mater. Res. 41, 99-132 10.1146/annurev-matsci-062910-100429
3. Moulay, S. (2014) Dopa/catechol-tethered polymers: Bioadhesives and biomimetic adhesive materials Polym. Rev. 54, 436-513 10.1080/15583724.2014.881373
4. Stewart, R. J., Ransom, T. C., and Hlady, V. (2011) Natural underwater adhesives J. Polym. Sci., Part B: Polym. Phys. 49, 757-771 10.1002/polb.22256
5. 2 surfaces: The effect of pH Biomacromolecules 14, 1072-1077 10.1021/bm301908y
6. Lee, H., Scherer, N. F., and Messersmith, P. B. (2006) Single-molecule mechanics of mussel adhesion Proc. Natl. Acad. Sci. U. S. A. 103, 12999-13003 10.1073/pnas.0605552103
7. Ahn, K., Lee, D. W., Israelachvili, J. N., and Waite, J. H. (2014) Surface-initiated self-healing of polymers in aqueous media Nat. Mater. 13, 867-872 10.1038/nmat4037
8. 3+-mediated bridging between dopa-containing protein films in water Proc. Natl. Acad. Sci. U. S. A. 107, 12850-12853 10.1073/pnas.1007416107
9. Nemes, Z., Marekov, L. N., and Steinert, P. M. (1999) Involucrin cross-linking by transglutaminase 1 J. Biol. Chem. 274, 11013-11021 10.1074/jbc.274.16.11013
10. Yu, J., Wei, W., Danner, E., Israelachvili, J. N., and Waite, J. H. (2011) Effects of interfacial redox in mussel adhesive protein films on mica Adv. Mater. 23, 2362-2366 10.1002/adma.201003580
11. Danner, E. W., Kan, Y., Hammer, M. U., Israelachvili, J. N., and Waite, J. H. (2012) Adhesion of mussel foot protein mefp-5 to mica: An underwater superglue Biochemistry 51, 6511-6518 10.1021/bi3002538
12. Yu, J., Wei, W., Danner, E. W., Ashley, R. K., Israelachvili, J. N., and Waite, J. H. (2011) Mussel protein adhesion depends on interprotein thiol-mediated redox modulation Nat. Chem. Biol. 7, 588-590 10.1038/nchembio.630
13. Rzepecki, L. M., Nagafuchi, T., and Waite, J. H. (1991) α,β-Dehydro-3,4-dihydroxyphenylalanine derivatives: Potential sclerotization intermediates in natural composite materials Arch. Biochem. Biophys. 285, 17-26 10.1016/0003-9861(91)90323-B
14. Rzepecki, L. M. and Waite, J. H. (1991) α,β-Dehydro-3,4-dihydroxyphenylalanine derivatives: Rate and mechanism of formation Arch. Biochem. Biophys. 285, 27-36 10.1016/0003-9861(91)90324-C
15. Kan, Y., Danner, E. W., Israelachvili, J. N., Chen, Y., and Waite, J. H. (2014) Boronate complex formation with Dopa containing mussel adhesive protein retards pH-induced oxidation and enables adhesion to mica PLoS One 9 (10) e108869 10.1371/journal.pone.0108869
16. Ramagopal, U. A., Ramakumar, S., Mathur, P., Joshi, R., and Chauhan, V. S. (2002) Dehydrophenylalanine zippers: strong helix-helix clamping through a network of weak interactions Protein Eng., Des. Sel. 15, 331-335 10.1093/protein/15.4.331
17. Sugumaran, M., Duggaraju, P., Jayachandran, E., and Kirk, K. L. (1999) Formation of a new quinone methide intermediate during the oxidative transformation of 3,4-dihydroxyphenylacetic acids: implication for eumelanin biosynthesis Arch. Biochem. Biophys. 371, 98-106 10.1006/abbi.1999.1420
18. Janes, S. M., Mu, D., Wemmer, D., Smith, A. J., Kaur, S., Maltby, D., Burlingame, A. L., and Klinman, J. P. (1990) A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase Science 248, 981-987 10.1126/science.2111581
19. Grotzinger, E. and Campbell, I. M. (1972) Intermediate symmetry in lawsone biosynthesis Phytochemistry 11, 675-679 10.1016/0031-9422(72)80031-1
20. Sugumaran, M., Semensi, V., Kalyanaraman, B., Bruce, J. M., and Land, E. J. J. (1992) Evidence for the formation of a quinone methide during the oxidation of the insect cuticular sclerotizing precursor 1,2-dehydro-N-acetyldopamine J. Biol. Chem. 267, 10355-10361
21. Paez, J. I., Ustahüseyin, O., Serrano, C., Ton, X., Shafiq, Z., Auernhammer, G. K., d'Ischia, M., and del Campo, A. (2015) Gauging and tuning cross-linking kinetics of catechol-PEG adhesives via catecholamine functionalization Biomacromolecules 16, 3811-3818 10.1021/acs.biomac.5b01126
22. Abebe, A., Kuang, Q. F., Evans, J. J., and Sugumaran, M. (2013) Mass spectrometric studies shed light on unusual oxidative transformations of 1,2-dehydro-N-acetyldopa Rapid Commun. Mass Spectrom. 27, 1785-1793 10.1002/rcm.6630
23. Sugumaran, M. and Ricketts, D. (1995) Model sclerotization studies. 3. Cuticular enzyme catalyzed oxidation of peptidyl model tyrosine and dopa derivatives Arch. Insect Biochem. Physiol. 28, 17-32 10.1002/arch.940280103
24. Sugumaran, M., Giglio, L., Kundzicz, H., Saul, S., and Semensi, V. (1992) Studies on the enzymes involved in puparial cuticle sclerotization in Drosophila melanogaster Arch. Insect Biochem. Physiol. 19, 271-283 10.1002/arch.940190406
25. Bard, A. J. and Faulkner, L. R. (2001) Electrochemical methods: Fundamentals and applications, 2nd ed., Chapter 6, Wiley, New York.
26. Ewing, A. G., Bigelow, J. C., and Wightman, R. M. (1983) Direct in vivo monitoring of dopamine released from two striatal compartments in the rat Science 221, 169-171 10.1126/science.6857277
27. Imazu, S., Shimohigashi, Y., Kodama, H., Sakaguchi, K., Waki, M., Kato, T., and Izumiya, N. (1988) Conformationally stabilized gramicidin S analog containing dehydrophenylalanine in place of D-phenylalanine Int. J. Pept. Protein Res. 32, 298-30 10.1111/j.1399-3011.1988.tb01264.x
28. Susi, H. and Byler, D. M. (1986) Resolution-enhanced Fourier transform infrared spectroscopy of enzymes Methods Enzymol. 130, 290-311 10.1016/0076-6879(86)30015-6
29. Zheng, B., Cheng, S., Liu, W., Lam, M. H.-W., and Liang, H. (2013) Small organic molecules detection based on aptamer-modified gold nanoparticles-enhanced quartz crystal microbalance with dissipation biosensor Anal. Biochem. 438, 144-149 10.1016/j.ab.2013.03.030
30. Wei, W., Yu, J., Broomell, C., Israelachvili, J. N., and Waite, J. H. (2013) Hydrophobic enhancement of Dopa-mediated adhesion in a mussel foot protein J. Am. Chem. Soc. 135, 377-383 10.1021/ja309590f
31. Ashkenazi, N., Vigalok, A., Parthiban, S., Ben-David, Y., Shimon, L. J. W., Martin, J. M. L., and Milstein, D. J. (2000) Discovery of the first metallaquinone J. Am. Chem. Soc. 122, 8797-8798 10.1021/ja001759d