CoChat
Sign Up
Cited by 632Polymer Surface Interaction StudiesMarine Biology and Environmental ChemistryHydrogels: synthesis, properties, applications

Recent approaches in designing bioadhesive materials inspired by mussel adhesive protein

Open access
Kord Forooshani, Pegah, Lee, Bruce P.·2017·Journal of Polymer Science Part A: Polymer Chemistry
DOI 10.1002/pola.28368PMC PMC5132118
Open this paper in CoChat — free accountOpen PDF

Abstract

Marine mussels secret protein‐based adhesives, which enable them to anchor to various surfaces in a saline, intertidal zone. Mussel foot proteins (Mfps) contain a large abundance of a unique, catecholic amino acid, Dopa, in their protein sequences. Catechol offers robust and durable adhesion to various substrate surfaces and contributes to the curing of the adhesive plaques. In this article, we review the unique features and the key functionalities of Mfps, catechol chemistry, and strategies for preparing catechol‐functionalized polymers. Specifically, we reviewed recent findings on the contributions of various features of Mfps on interfacial binding, which include coacervate formation, surface drying properties, control of the oxidation state of catechol, among other features. We also summarized recent developments in designing advanced biomimetic materials including coacervate‐forming adhesives, mechanically improved nano‐ and micro‐composite adhesive hydrogels, as well as smart and self‐healing materials. Finally, we review the applications of catechol‐functionalized materials for the use as biomedical adhesives, therapeutic applications, and antifouling coatings. © 2016 The Authors. Journal of Polymer Science Part A: Polymer Chemistry Published by Wiley Periodicals, Inc. J. Polym. Sci., Part A: Polym. Chem. 2017 , 55 , 9–33

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1002/pola.28368

Cites

3 of 3 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Many methods have been developed to incorporate the catechol group into polymers, including incorporation by classic organic reactions, polymerization of catechol-based monomers, and biosynthesis of catechol-containing proteins.

    “During recent decades, many methods have been developed to incorporate the catechol group into polymers [4,47], including the incorporation of the catechol group by classic organic reactions, polymerization of catechol-based monomers, and biosynthesis of catechol-containing proteins (Figure 3).”

    From Mussel-Inspired Injectable Adhesive Hydrogels for Biomedical Applications (2024) · cites this paper as [4]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 277

  1. [1]J. H. Waite, Int. J. Adhes. Adhes. 1987, 7, 9– 14.
  2. [2]J. Waite, Chem. Ind. 1991, 2, 607– 611.
  3. [3]E. W. Danner, Y. Kan, M. U. Hammer, J. N. Israelachvili, J. H. Waite, Biochemistry 2012, 51, 6511– 6518. 22873939 PMC3428132
  4. [4]W. Wei, J. Yu, C. Broomell, J. N. Israelachvili, J. H. Waite, J. Am. Chem. Soc. 2012, 135, 377– 383. 23214725 PMC3587158
  5. [5]J. H. Waite, S. O. Andersen, Biochim. Biophys. Acta. 1978, 541, 107– 114.
  6. [6]L. Ninan, J. Monahan, R. L. Stroshine, J. J. Wilker, R. Shi, Biomaterials 2003, 24, 4091– 4099. 12834605
  7. [7]L. O. Burzio, V. A. Burzio, T. Silva, L. A. Burzio, J. Pardo, Curr. Opin. Biotechnol. 1997, 8, 309– 312. 9206011
  8. [8]B. P. Lee, P. B. Messersmith, J. N. Israelachvili, J. H. Waite, Annu. Rev. Mater. Res. 2011, 41, 99. 22058660 PMC3207216
  9. [9]A. Hagenau, M. H. Suhre, T. R. Scheibel, Prog. Polym. Sci. 2014, 39, 1564– 1583.
  10. [10]E. Faure, C. Falentin‐Daudré, C. Jérôme, J. Lyskawa, D. Fournier, P. Woisel, C. Detrembleur, Prog. Polym. Sci. 2013, 38, 236– 270.
  11. [11]J. H. Waite, Ann. NY Acad. Sci. 1999, 875, 301– 309. 10415577
  12. [12]E. Bell, J. Gosline, J. Exp. Biol. 1996, 199, 1005– 1017. 9318809
  13. [13]J. D. Witman, T. H. Suchanek, Mar. Ecol. Prog. Ser. 1984, 16, 259– 268.
  14. [14]H. Zhao, J. H. Waite, J. Biol. Chem. 2006, 281, 26150– 26158. 16844688
  15. [15]Y. Yao, K. Khoo, M. Chung, S. Li, J. Chromatogr. A 1994, 680, 431– 435.
  16. [16]D. R. Filpula, S. M. Lee, R. P. Link, S. L. Strausberg, R. L. Strausberg, Biotechnol. Prog. 1990, 6, 171– 177. 1367451
  17. [17]C. V. Benedict, J. H. Waite, J. Morphol. 1986, 189, 261– 270. 3772980
  18. [18]L. M. Rzepecki, K. M. Hansen, J. H. Waite, Biol. Bull. 1992, 183, 123– 137. 29304577
  19. [19]H. Zhao, J. H. Waite, Biochemistry 2006, 45, 14223– 14231. 17115717 PMC1892233
  20. [20]X. Qin, J. H. Waite, J. Exp. Biol. 1995, 198, 633– 644. 7714453
  21. [21]X. X. Qin, J. H. Waite, Proc. Natl. Acad. Sci. USA. 1998, 95, 10517– 10522. 9724735 PMC27926
  22. [22]S. Warner, J. Waite, Marine Biol. 1999, 134, 729– 734.
  23. [23]V. V. Papov, T. V. Diamond, K. Biemann, J. H. Waite, J. Biol. Chem. 1995, 270, 20183– 20192. 7650037
  24. [24]H. Zhao, N. B. Robertson, S. A. Jewhurst, J. H. Waite, J. Biol. Chem. 2006, 281, 11090– 11096. 16495227
  25. [25]R. Y. Floriolli, J. von Langen, J. H. Waite, Marine Biotechnol. 2000, 2, 352– 363. 10960125
  26. [26]J. H. Waite, X. Qin, Biochemistry 2001, 40, 2887– 2893. 11258900
  27. [27]G. Proudfoot, I. Ritchie, Aust. J. Chem. 1983, 36, 885– 894.
  28. [28]H. G. Silverman, F. F. Roberto, Marine Biotechnol. 2007, 9, 661– 681. PMC2100433 17990038
  29. [29]J. R. Long, J. L. Dindot, H. Zebroski, S. Kiihne, R. H. Clark, A. A. Campbell, P. S. Stayton, G. P. Drobny, Proc. Natl. Acad. Sci. USA. 1998, 95, 12083– 12087. 9770443 PMC22788
  30. [30]J. Yu, In Adhesive Interactions of Mussel Foot Proteins; Springer; 2014, pp 31–41.
  31. [31]J. H. Waite, M. L. Tanzer, Science 1981, 212, 1038– 1040. 17779975
  32. [32]J. Schnurrer, C. M. Lehr, Int. J. Pharm. 1996, 141, 251– 256.
  33. [33]N. D. Catron, H. Lee, P. B. Messersmith, Biointerphases 2006, 1, 134– 141. 20408626
  34. [34]W. M. Chirdon, W. J. O'Brien, R. E. Robertson, J. Biomed. Mater. Res. Part B: Appl. Biomater. 2003, 66, 532– 538. 12861604
  35. [35]T. L. Coombs, P. J. Keller, Aquatic Toxicol.. 1981, 1, 291– 300.
  36. [36]A. M. Baty, P. K. Leavitt, C. A. Siedlecki, B. J. Tyler, P. A. Suci, R. E. Marchant, G. G. Geesey, Langmuir 1997, 13, 5702– 5710.
  37. [37]B. R. Baker, A. N. Laiwalla, J. Y. Yoon, J. Canavate, R. L. Garrell, Polym. Mater. Sci. Eng. 2001, 85, 115– 116.
  38. [38]J. P. Gallivan, D. A. Dougherty, J. Am. Chem. Soc. 2000, 122, 870–874.
  39. [39]J. P. Gallivan, D. A. Dougherty, J. Am. Chem. Soc. 2000, 122, 870– 874.
  40. [40]Q. Lu, D. X. Oh, Y. Lee, Y. Jho, D. S. Hwang, H. Zeng, Angew. Chem. Int. Ed. 2013, 52, 3944– 3948. 23450629
  41. [41]K. V. Pillai, S. Renneckar, Biomacromolecules 2009, 10, 798– 804. 19226174
  42. [42]S. Das, N. R. M. Rodriguez, W. Wei, J. H. Waite, J. N. Israelachvili, Adv. Funct. Mater. 2015, 25, 5840– 5847. PMC5488267 28670243
  43. [43]S. Kim, A. Faghihnejad, Y. Lee, Y. Jho, H. Zeng, D. S. Hwang, J. Mater. Chem. B 2015, 3, 738– 743. 32262163
  44. [44]W. Wei, J. Yu, M. A. Gebbie, Y. Tan, N. R. Martinez Rodriguez, J. N. Israelachvili, J. H. Waite, Langmuir 2015, 31, 1105– 1112. 25540823 PMC4310636
  45. [45]D. S. Hwang, H. Zeng, Q. Lu, J. Israelachvili, J. H. Waite, Soft Matter 2012, 8, 5640– 5648. 23105946 PMC3482130
  46. [46]M. J. Sever, J. J. Wilker, Dalton Trans. 2006, 14, 813– 822. 16437176
  47. [47]C. A. Tyson, A. E. Martell, J. Am. Chem. Soc. 1968, 90, 3379– 3386. 5651561
  48. [48]B. A. Borgias, S. R. Cooper, Y. B. Koh, K. N. Raymond, Inorg. Chem. 1984, 23, 1009– 1016.
  49. [49]L. Sommer, Z. Anorg. Allg. Chem. 1963, 321, 191– 197.
  50. [50]C. Morlay, M. Cromer, Y. Mouginot, O. Vittori, Talanta 1998, 45, 1177– 1188. 18967110
  51. [51]O. K. Borggaard, Acta Chem. Scand. 1972, 26, 393– 395. 4647674
  52. [52]S. W. Taylor, G. W. Luther, III, J. H. Waite, Inorg. Chem. 1994, 33, 5819– 5824.
  53. [53]S. W. Taylor, D. B. Chase, M. H. Emptage, M. J. Nelson, J. H. Waite, Inorg. Chem. 1996, 35, 7572– 7577.
  54. [54]M. J. Harrington, A. Masic, N. Holten‐Andersen, J. H. Waite, P. Fratzl, Science. 2010, 328, 216– 220. 20203014 PMC3087814
  55. [55]M. J. Harrington, H. S. Gupta, P. Fratzl, J. H. Waite, J. Struct. Biol. 2009, 167, 47– 54. 19275941 PMC2692767
  56. [56]N. Holten‐Andersen, M. J. Harrington, H. Birkedal, B. P. Lee, P. B. Messersmith, K. Y. C. Lee, J. H. Waite, Proc. Natl. Acad. Sci. USA. 2011, 108, 2651– 2655. 21278337 PMC3041094
  57. [57]N. Holten‐Andersen, A. Jaishankar, M. J. Harrington, D. E. Fullenkamp, G. DiMarco, L. He, G. H. McKinley, P. B. Messersmith, K. Y. C. Lee, J. Mater. Chem. B 2014, 2, 2467– 2472. PMC4582448 26413297
  58. [58]M. Krogsgaard, M. A. Behrens, J. S. Pedersen, H. Birkedal, Biomacromolecules 2013, 14, 297– 301. 23347052
  59. [59]B. J. Kim, H. Cheong, B. H. Hwang, H. J. Cha, Angew. Chem. 2015, 127, 7426– 7430.
  60. [60]B. P. Lee, A. Narkar, R. Wilharm, Sens. Actuator. B: Chem. 2016, 227, 248– 254.
  61. [61]B. P. Lee, M. H. Lin, A. Narkar, S. Konst, R. Wilharm, Sen. Actuator. B: Chem. 2015, 206, 456– 462.
  62. [62]B. P. Lee, S. Konst, Adv. Mater. 2014, 26, 3415– 3419. 24596273
  63. [63]B. J. Kim, S. Kim, D. X. Oh, A. Masic, H. J. Cha, D. S. Hwang, J. Mater. Chem. B. 2015, 3, 112– 118. 32261931
  64. [64]M. Krogsgaard, A. Andersen, H. Birkedal, Chem. Commun. 2014, 50, 13278– 13281. 25229074
  65. [65]R. Kummert, W. Stumm, J. Colloid Interface Sci. 1980, 75, 373– 385.
  66. [66]B. P. Lee, C. Y. Chao, F. N. Nunalee, E. Motan, K. R. Shull, P. B. Messersmith, Macromolecules 2006, 39, 1740– 1748.
  67. [67]M. P. Soriaga, A. T. Hubbard, J. Am. Chem. Soc. 1982, 104, 3937– 3945.
  68. [68]H. Lee, N. F. Scherer, P. B. Messersmith, Proc. Natl. Acad. Sci. USA. 2006, 103, 12999– 13003. 16920796 PMC1559742
  69. [69]S. A. Mian, X. Gao, S. Nagase, J. Jang, Theor. Chem. Acc. 2011, 130, 333– 339.
  70. [70]S. A. Mian, L. C. Saha, J. Jang, L. Wang, X. Gao, S. Nagase, J. Phys. Chem. C 2010, 114, 20793– 20800.
  71. [71]J. L. Dalsin, B. H. Hu, B. P. Lee, P. B. Messersmith, J. Am. Chem. Soc. 2003, 125, 4253– 4258. 12670247
  72. [72]J. L. Dalsin, L. Lin, P. B. Messersmith, Polym. Mater. Sci. Eng. Preprints 2004, 90, 247– 248.
  73. [73]J. L. Dalsin, L. Lin, S. Tosatti, J. Vörös, M. Textor, P. B. Messersmith, Langmuir. 2005, 21, 640– 646. 15641834
  74. [74]J. Yu, W. Wei, M. S. Menyo, A. Masic, J. H. Waite, J. N. Israelachvili, Biomacromolecules 2013, 14, 1072– 1077. 23452271 PMC3635841
  75. [75]L. M. McDowell, L. A. Burzio, J. H. Waite, J. Schaefer, J. Biol. Chem. 1999, 274, 20293– 20295. 10400649
  76. [76]L. M. Rzepecki, T. Nagafuchi, J. H. Waite, Arch. Biochem. Biophys. 1991, 285, 17– 26. 1846730
  77. [77]B. P. Lee, J. L. Dalsin, P. B. Messersmith, Biomacromolecules 2002, 3, 1038– 1047. 12217051
  78. [78]J. H. Waite, Comp. Biochem. Physiol. Part B: Biochem. Mol. Biol. 1990, 97, 19– 29. 2123765
  79. [79]M. Sugumaran, H. Dali, V. Semensi, Arch. Insect Biochem. Physiol. 1989, 11, 127– 137. 1799672
  80. [80]H. Lee, S. M. Dellatore, W. M. Miller, P. B. Messersmith, Science 2007, 318, 426– 430. 17947576 PMC2601629
  81. [81]C. Cheng, S. Li, S. Nie, W. Zhao, H. Yang, S. Sun, C. Zhao, Biomacromolecules 2012, 13, 4236– 4246. 23152977
  82. [82]Y. Ren, J. G. Rivera, L. He, H. Kulkarni, D.‐K. Lee, P. B. Messersmith, BMC Biotechnol. 2011, 11, 1– 8. 21649934 PMC3212977
  83. [83]K. C. Black, J. Yi, J. G. Rivera, D. C. Zelasko‐Leon, P. B. Messersmith, Nanomedicine 2013, 8, 17– 28. 22891865 PMC3530415
  84. [84]C. Lim, J. Huang, S. Kim, H. Lee, H. Zeng, D. S. Hwang, Angew. Chem. Int. Ed. 2016, 55, 3342– 3346. 26833974
  85. [85]S. M. Kang, N. S. Hwang, J. Yeom, S. Y. Park, P. B. Messersmith, I. S. Choi, R. Langer, D. G. Anderson, H. Lee, Adv. Funct. Mater. 2012, 22, 2949– 2955. 23580891 PMC3619432
  86. [86]S. Kim, J.‐M. Moon, J. S. Choi, W. K. Cho, S. M. Kang, Adv. Funct. Mater., 2016, 26, 4099– 4105.
  87. [87]M. M. Cencer, Y. Liu, A. Winter, M. Murley, H. Meng, B. P. Lee, Biomacromolecules 2014, 15, 2861– 2869. 25010812 PMC4130238
  88. [88]J. Li, B. M. Christensen, J. Electroanal. Chem. 1994, 375, 219– 231.
  89. [89]I. F. Tannock, D. Rotin, Cancer Res. 1989, 49, 4373– 4384. 2545340
  90. [90]H. Ohman, A. Vahlquist, Acta Derm. Venereol. 1994, 74, 375– 379. 7817676
  91. [91]B. R. Soller, R. H. Micheels, J. Coen, B. Parikh, L. Chu, C. Hsi, J. Clin. Monitor. Comput. 1996, 12, 387– 395. 8934345
  92. [92]B. R. Soller, T. Khan, J. Favreau, C. Hsi, J. C. Puyana, S. O. Heard, J. Surg. Res. 2003, 114, 195– 201. 14559446
  93. [93]H. Meng, Y. Li, M. Faust, S. Konst, B. P. Lee, Acta Biomater. 2015, 17, 160– 169. 25676582 PMC4380612
  94. [94]M. Mochizuki, S. Yamazaki, K. Kano, T. Ikeda, Biochim. Biophys. Acta (BBA) Gen. Subjects 2002, 1569, 35– 44. 11853955
  95. [95]P. Chelikani, I. Fita, P. C. Loewen, CMLS, Cell. Mol. Life Sci. 2004, 61, 192– 208. 14745498 PMC11138816
  96. [96]N. Brian, H. Ahswin, N. Smart, Y. Bayon, S. Wohlert, J. A. Hunt, Eur. Cells Mater. 2012, 24, 249– 265. 23007910
  97. [97]A. M. Cooper, B. H. Segal, A. A. Frank, S. M. Holland, I. M. Orme, Infect. Immun. 2000, 68, 1231– 1234. 10678931 PMC97272
  98. [98]A. E. K. Loo, Y. T. Wong, R. Ho, M. Wasser, T. Du, W. T. Ng, B. Halliwell, PLoS One 2012, 7, e49215. 23152875 PMC3496701
  99. [99]S. Chigurupati, M. R. Mughal, E. Okun, S. Das, A. Kumar, M. McCaffery, S. Seal, M. P. Mattson, Biomaterials 2013, 34, 2194– 2201. 23266256 PMC3552035
  100. [100]N. R. Martinez Rodriguez, S. Das, Y. Kaufman, J. N. Israelachvili, J. H. Waite, Biofouling 2015, 31, 221– 227. 25875963 PMC4420479
  101. [101]R. Stewart, T. Ransom, V. Hlady. J. Polym. Sci. Part B: Polym. Phys. 2011, 49, 757–771. PMC3104275 21643511
  102. [102]J. Yu, W. Wei, E. Danner, R. K. Ashley, J. N. Israelachvili, J. H. Waite, Nat. Chem. Biol. 2011, 7, 588– 590. 21804534 PMC3158268
  103. [103]J. H. Ortony, D. S. Hwang, J. M. Franck, J. H. Waite, S. Han, Biomacromolecules 2013, 14, 1395– 1402. 23540713 PMC4090114
  104. [104]M. Yu, J. Hwang, T. J. Deming, J. Am. Chem. Soc. 1999, 121, 5825– 5826.
  105. [105]J. Yu, W. Wei, E. Danner, J. N. Israelachvili, J. H. Waite, Adv. Mater. 2011, 23, 2362– 2366. 21520458 PMC3221558
  106. [106]G. Springsteen, B. Wang, Tetrahedron 2002, 58, 5291– 5300.
  107. [107]M. Guvendiren, D. A. Brass, P. B. Messersmith, K. R. Shull, J. Adhes. 2009, 85, 631– 645. 21461121 PMC3066440
  108. [108]S. C. Nicklisch, J. E. Spahn, H. Zhou, C. M. Gruian, J. H. Waite, Biochemistry 2016, 55, 2022– 2030. 26998552 PMC4934423
  109. [109]C. G. De Kruif, F. Weinbreck, R. de Vries, Curr Opin Colloid Interface Sci. 2004, 9, 340– 349.
  110. [110]S. Seo, S. Das, P. J. Zalicki, R. Mirshafian, C. D. Eisenbach, J. N. Israelachvili, J. H. Waite, B. K. Ahn, J. Am. Chem. Soc. 2015, 137, 9214– 9217. 26172268
  111. [111]B. K. Ahn, S. Das, R. Linstadt, Y. Kaufman, N. R. Martinez‐Rodriguez, R. Mirshafian, E. Kesselman, Y. Talmon, B. H. Lipshutz, J. N. Israelachvili, J. H. Waite, Nat. Commun. 2015, 6, 8663. 26478273 PMC4667698
  112. [112]W. Wei, Y. Tan, N. R. M. Rodriguez, J. Yu, J. N. Israelachvili, J. H. Waite, Acta Biomater. 2014, 10, 1663– 1670. 24060881 PMC3960351
  113. [113]S. Kim, J. Huang, Y. Lee, S. Dutta, H. Y. Yoo, Y. M. Jung, Y. Jho, H. Zeng, D. S. Hwang, Proc. Natl. Acad. Sci. USA. 2016, 113, E847– E853. 26831090 PMC4763778
  114. [114]R. Moulds, T. Baldwin, Int. J. Adhes. Adhes. 1983, 3, 203– 207.
  115. [115]Y. Akdogan, W. Wei, K. Y. Huang, Y. Kageyama, E. W. Danner, D. R. Miller, N. R. Martinez Rodriguez, J. H. Waite, S. Han, Angew. Chem. 2014, 126, 11435– 11438. PMC4198389 25168789
  116. [116]W. Wei, L. Petrone, Y. Tan, H. Cai, J. N. Israelachvili, A. Miserez, J. H. Waite, Adv. Funct. Mater. 2016, 26, 3496– 3507. 27840600 PMC5102340
  117. [117]Q. Lin, D. Gourdon, C. Sun, N. Holten‐Andersen, T. H. Anderson, J. H. Waite, J. N. Israelachvili, Proc. Natl. Acad. Sci. USA. 2007, 104, 3782– 3786. 17360430 PMC1820661
  118. [118]J. Yu, Y. Kan, M. Rapp, E. Danner, W. Wei, S. Das, D. R. Miller, Y. Chen, J. H. Waite, J. N. Israelachvili, Proc. Natl. Acad. Sci. USA. 2013, 110, 15680– 15685. 24014592 PMC3785749
  119. [119]G. P. Maier, M. V. Rapp, J. H. Waite, J. N. Israelachvili, A. Butler, Science 2015, 349, 628– 632. 26250681
  120. [120]C. J. Sun, A. Srivastava, J. R. Reifert, J. H. Waite, J. Adhes. 2009, 85, 126– 138. 20126508 PMC2757296
  121. [121]M. Cencer, M. Murley, Y. Liu, B. P. Lee, Biomacromolecules 2015, 16, 404– 410. 25495043 PMC4294588
  122. [122]X. Ding, G. K. Vegesna, H. Meng, A. Winter, B. P. Lee, Macromol. Chem. Phys. 2015, 216, 1109– 1119. 26929588 PMC4768752
  123. [123]E. Amstad, A. U. Gehring, H. Fischer, V. V. Nagaiyanallur, G. Hahner, M. Textor, E. Reimhult, J. Phys. Chem. C 2011, 115, 683– 691.
  124. [124]E. Amstad, T. Gillich, I. Bilecka, M. Textor, E. Reimhult, Nano Lett. 2009, 9, 4042– 4048. 19835370
  125. [125]M. S. Menyo, C. J. Hawker, J. H. Waite, Soft Matter 2013, 9, 10314– 10323. PMC3838863 24285981
  126. [126]J. Anderson, M.‐H. Lin, C. Privette, M. Flowers, M. Murley, B. P. Lee, K. G. Ong, ScienceJet 2015, 4, 1–14. PMC4335653 25710000
  127. [127]Z. Shafiq, J. Cui, L. Pastor‐Pérez, V. San Miguel, R. A. Gropeanu, C. Serrano, A. del Campo, Angew. Chem. Int. Ed. 2012, 51, 4332– 4335. 22461306
  128. [128]L. García‐Fernández, J. Cui, C. Serrano, Z. Shafiq, R. A. Gropeanu, V. S. Miguel, J. I. Ramos, M. Wang, G. K. Auernhammer, S. Ritz, A. A. Golriz, R. Berger, M. Wagner, A. del Campo, Adv. Mater. 2013, 25, 529– 533. 23139083
  129. [129]H. Ejima, J. J. Richardson, K. Liang, J. P. Best, M. P. van Koeverden, G. K. Such, J. Cui, F. Caruso, Science 2013, 341, 154– 157. 23846899
  130. [130]J. Guo, H. Sun, K. Alt, B. L. Tardy, J. J. Richardson, T. Suma, H. Ejima, J. Cui, C. E. Hagemeyer, F. Caruso, Adv. Healthcare Mater. 2015, 4, 1796– 1801. 26088356
  131. [131]D. G. Barrett, T. S. Sileika, P. B. Messersmith, Chem. Commun. 2014, 50, 7265– 7268. PMC4146571 24871486
  132. [132]G. Shen, R. Xing, N. Zhang, C. Chen, G. Ma, X. Yan, ACS Nano, 2016, 10, 5720– 5729. 27223166
  133. [133]Z. Liu, B. H. Hu, P. B. Messersmith, Tetrahedron Lett. 2008, 49, 5519– 5521. 19759805 PMC2598405
  134. [134]K. C. L. Black, Z. Liu, P. B. Messersmith, Chem. Mater. 2011, 23, 1130– 1135. 21666825 PMC3109993
  135. [135]G. Westwood, T. N. Horton, J. J. Wilker, Maclomolecules 2007, 40, 3960– 3964.
  136. [136]B. H. Hu, P. B. Messersmith, Tetrahedron Lett. 2000, 41, 5795– 5798.
  137. [137]M. Yu, T. J. Deming, Macromolecules 1998, 31, 4739– 4745. 9680407
  138. [138]B. P. Lee, K. Huang, F. N. Nunalee, K. R. Shull, P. B. Messersmith, J. Biomater. Sci. Polym. Ed. 2004, 15, 449– 464. 15212328
  139. [139]H. Lee, B. P. Lee, P. B. Messersmith, Nature 2007, 448, 338– 341. 17637666
  140. [140]J. Heo, T. Kang, S. G. Jang, D. S. Hwang, J. M. Spruell, K. L. Killops, J. H. Waite, C. J. Hawker, J. Am. Chem. Soc. 2012, 134, 20139– 20145. 23181614 PMC3521601
  141. [141]H. Nam, M. M. Kim, Food Chem. Toxicol. 2013, 55, 106– 112. 23313798
  142. [142]S. F. Hamed, Z. Sadek, A. Edris, J. Oleo Sci. 2012, 61, 641– 648. 23138253
  143. [143]T. F. Bachiega, J. P. B. de Sousa, J. K. Bastos, J. M. Sforcin, J. Pharm. Pharmacol. 2012, 64, 610– 616. 22420667
  144. [144]A. Almaroof, S. Niazi, L. Rojo, F. Mannocci, S. Deb, Dent. Mater. 2016, 32, 929– 939. 27130610
  145. [145]A. Almaroof, L. Rojo, F. Mannocci, S. Deb, Dent. Mater. 2016, 32, 149– 160. 26777114
  146. [146]K. Huang, B. P. Lee, D. R. Ingram, P. B. Messersmith, Biomacromolecules 2002, 3, 397– 406. 11888328
  147. [147]M. Mehdizadeh, H. Weng, D. Gyawali, L. Tang, J. Yang, Biomaterials 2012, 33, 7972– 7983. 22902057 PMC3432175
  148. [148]C. E. Brubaker, H. Kissler, L. J. Wang, D. B. Kaufman, P. B. Messersmith, Biomaterials 2010, 31, 420– 427. 19811819 PMC2783676
  149. [149]M. Perrini, D. Barrett, N. Ochsenbein‐Koelble, R. Zimmermann, P. Messersmith, M. Ehrbar, J. Mech. Behav. Biomed. Mater., 2016, 58, 57– 64. 26255212
  150. [150]J. L. Murphy, L. Vollenweider, F. Xu, B. P. Lee, Biomacromolecules 2010, 11, 2976– 2984. 20919699 PMC3027843
  151. [151]B. Michael, V. Laura, L. M. John, X. Fangmin, L. Arinne, D. L. William, P. L. Bruce, Biomed. Mater. 2011, 6, 015014. 21266745
  152. [152]D. G. Barrett, G. G. Bushnell, P. B. Messersmith, Adv. Healthcare Mater. 2013, 2, 745– 755. PMC3685437 23184616
  153. [153]M. Guvendiren, P. B. Messersmith, K. R. Shull, Biomacromolecules 2008, 9, 122– 128. 18047285 PMC3066146
  154. [154]P. Sun, J. Wang, X. Yao, Y. Peng, X. Tu, P. Du, Z. Zheng, X. Wang, ACS Appl. Mater. Interfaces 2014, 6, 12495– 12504. 25017583
  155. [155]J. Y. Park, J. Yeom, J. S. Kim, M. Lee, H. Lee, Y. S. Nam, Macromol. Biosci. 2013, 13, 1511– 1519. 23904239
  156. [156]K. Kim, J. H. Ryu, D. Y. Lee, H. Lee, Biomater. Sci. 2013, 1, 783– 790. 32481831
  157. [157]A. I. Neto, A. C. Cibrão, C. R. Correia, R. R. Carvalho, G. M. Luz, G. G. Ferrer, G. Botelho, C. Picart, N. M. Alves, J. F. Mano, Small 2014, 10, 2459– 2469. 24616168
  158. [159]C. Lee, J. Shin, J. S. Lee, E. Byun, J. H. Ryu, S. H. Um, D. I. Kim, H. Lee, S. W. Cho, Biomacromolecules 2013, 14, 2004– 2013. 23639096
  159. [160]T. Kang, X. Banquy, J. H. Heo, C. N. Lim, N. A. Lynd, P. Lundberg, D. X. Oh, H. K. Lee, Y. K. Hong, D. S. Hwang, J. H. Waite, J. N. Israelachvili, C. J. Hawker, Acs Nano 2016, 10, 930– 937. 26695175 PMC4932843
  160. [161]K. M. Mattson, A. A. Latimer, A. J. McGrath, N. A. Lynd, P. Lundberg, Z. M. Hudson, C. J. Hawker, J. Polym. Sci. Part A: Polym. Chem. 2015, 53, 2685– 2692.
  161. [162]J. K. Sprafke, J. M. Spruell, K. M. Mattson, D. Montarnal, A. J. McGrath, R. Pötzsch, D. Miyajima, J. Hu, A. A. Latimer, B. I. Voit, J. Polym. Sci. Part A: Polym. Chem. 2015, 53, 319– 326.
  162. [163]A. Pechey, C. N. Elwood, G. R. Wignall, J. L. Dalsin, B. P. Lee, M. Vanjecek, I. Welch, R. Ko, H. Razvi, P. A. Cadieux, J. Urol. 2009, 182, 1628– 1636. 19683735 PMC2807180
  163. [164]H. Shao, K. N. Bachus, R. J. Stewart, Macromol. Biosci. 2009, 9, 464– 471. 19040222 PMC2848666
  164. [165]C. R. Matos‐Perez, J. D. White, J. J. Wilker, J. Am. Chem. Soc. 2012, 134, 9498– 9505. 22582754 PMC3415564
  165. [166]C. L. Jenkins, H. J. Meredith, J. J. Wilker, ACS Appl. Mater. Interfaces 2013, 5, 5091– 5096. 23668520
  166. [167]C. R. Matos‐Pérez, J. J. Wilker. Macromolecules 2012, 45, 6634– 6639. 23293396 PMC3534954
  167. [168]D. Leibig, A. H. Müller, H. Frey, Macromolecules 2016, 49, 4792– 4801.
  168. [169]S. Skelton, M. Bostwick, K. O'Connor, S. Konst, S. Casey, B. P. Lee, Soft Matter 2013, 9, 3825– 3833.
  169. [170]T. J. Deming, Nature 1997, 390, 386– 389. 9389476
  170. [171]K. Niederer, C. Schüll, D. Leibig, T. Johann, H. Frey, Macromolecules 2016, 49, 1655– 1665.
  171. [172]J. Liu, W. Yang, H. M. Zareie, J. J. Gooding, T. P. Davis, Macromolecules 2009, 42, 2931– 2939.
  172. [173]C. Zobrist, J. Sobocinski, J. Lyskawa, D. Fournier, V. Miri, M. Traisnel, M. Jimenez, P. Woisel, Macromolecules 2011, 44, 5883– 5892.
  173. [174]X. Fan, L. Lin, P. B. Messersmith, Biomacromolecules 2006, 7, 2443– 2448. 16903694
  174. [175]X. Fan, L. Lin, J. L. Dalsin, P. B. Messersmith, J. Am. Chem. Soc. 2005, 127, 15843– 15847. 16277527
  175. [176]C. Gao, G. Li, H. Xue, W. Yang, F. Zhang, S. Jiang, Biomaterials 2010, 31, 1486– 1492. 19962753
  176. [177]G. Li, G. Cheng, H. Xue, S. Chen, F. Zhang, S. Jiang, Biomaterials 2008, 29, 4592– 4597. 18819708
  177. [178]Q. Ye, X. Wang, S. Li, F. Zhou, Macromolecules 2010, 43, 5554– 5560.
  178. [179]J. Kuang, P. B. Messersmith, Langmuir 2012, 28, 7258– 7266. 22506651 PMC3351008
  179. [180]M. J. Sever, J. J. Wilker, Tetrahedron 2001, 57, 6139– 6146.
  180. [181]M. A. Behnam, T. R. Sundermann, C. D. Klein, Org. Lett. 2016, 18, 2016– 2019. 27104613
  181. [182]M. Bodanszky, Principles of Peptide Synthesis; Springer Science & Business Media: New York, 2012.
  182. [183]A. Akemi Ooka, R. L. Garrell, Biopolymers 2000, 57, 92– 102. 10766960
  183. [184]S. M. Miller, R. J. Simon, S. Ng, R. N. Zuckermann, J. M. Kerr, W. H. Moos, Drug Dev. Res. 1995, 35, 20– 32.
  184. [185]A. R. Statz, R. J. Meagher, A. E. Barron, P. B. Messersmith, J. Am. Chem. Soc. 2005, 127, 7972– 7973. 15926795
  185. [186]H. Zeng, D. S. Hwang, J. N. Israelachvili, J. H. Waite, Proc. Natl. Acad. Sci. USA. 2010, 107, 12850– 12853. 20615994 PMC2919964
  186. [187]D. S. Hwang, Y. Gim, H. J. Cha, Biotechnol. Prog. 2005, 21, 965– 970. 15932281
  187. [188]D. S. Hwang, H. J. Yoo, J. H. Jun, W. K. Moon, H. J. Cha, Appl. Environ Microbiol. 2004, 70, 3352– 3359. 15184131 PMC427802
  188. [189]D. S. Hwang, Y. Gim, H. J. Yoo, H. J. Cha, Biomaterials 2007, 28, 3560– 3568. 17507090
  189. [190]D. S. Hwang, H. Zeng, A. Srivastava, D. V. Krogstad, M. Tirrell, J. N. Israelachvili, J. H. Waite, Soft Matter 2010, 6, 3232– 3236. 21544267 PMC3085400
  190. [191]B. J. Kim, D. X. Oh, S. Kim, J. H. Seo, D. S. Hwang, A. Masic, D. K. Han, H. J. Cha, Biomacromolecules 2014, 15, 1579– 1585. 24650082
  191. [192]S. Lim, Y. S. Choi, D. G. Kang, Y. H. Song, H. J. Cha, Biomaterials 2010, 31, 3715– 3722. 20144475
  192. [193]C. Zhong, T. Gurry, A. A. Cheng, J. Downey, Z. Deng, C. M. Stultz, T. K. Lu, Nat Nano 2014, 9, 858– 866. PMC4191913 25240674
  193. [194]D. S. Hwang, S. B. Sim, H. J. Cha, Biomaterials 2007, 28, 4039– 4046. 17574667
  194. [195]J. J. Wilker, Nat. Chem. Biol. 2011, 7, 579– 580. 21849996
  195. [196]W. Wang, Y. Xu, A. Li, T. Li, M. Liu, R. von Klitzing, C. K. Ober, A. B. Kayitmazer, L. Li, X. Guo, RSC Adv. 2015, 5, 66871– 66878.
  196. [197]D. R. Miller, S. Das, K. Y. Huang, S. Han, J. N. Israelachvili, J. H. Waite, ACS Biomater. Sci. Eng. 2015, 1, 1121– 1128. 26618194 PMC4642218
  197. [198]M. R. Kim, T. G. Park, J. Controlled Release 2002, 80, 69– 77. 11943388
  198. [199]M. K. Jain, C. A. Grimes, Sens. Actuator. A: Phys. 2002, 100, 63– 69. 12398065
  199. [200]T. Wang, D. Liu, C. Lian, S. Zheng, X. Liu, Z. Tong, Soft Matter 2012, 8, 774– 783.
  200. [201]A. K. Gaharwar, S. A. Dammu, J. M. Canter, C. J. Wu, G. Schmidt, Biomacromolecules 2011, 12, 1641– 1650. 21413708

200 of 277 shown

Cited by

Sorted by citations

Authors
Kord Forooshani, P., & Lee, B. P.
Affiliations
  • Department of Biomedical Engineering Michigan Technological University Houghton Michigan 49931
  • Michigan Technological University (US)
Corresponding author
Lee, Bruce P.
ORCID
Lee, Bruce P.
Venue
Journal of Polymer Science Part A: Polymer Chemistry
Publisher
Wiley
Published
2016-10-11
Volume
55
Issue
1
Pages
9-33
ISSN
  • 0887-624X (ISSN-L)
  • 1099-0518
DOI
10.1002/pola.28368
PMC
PMC5132118
OpenAlex
W2531651920
Cited by
632
References
3
Citations by year
2026: 32 · 2025: 53 · 2024: 56 · 2023: 78 · 2022: 77 · 2021: 98 · 2020: 80 · 2019: 73 · 2018: 56 · 2017: 28
FWCI
2.94
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Polymer Science Part A Polymer Chemistry (publishedVersion, cc-by-nc-nd)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • Digital Commons - Michigan Tech (Michigan Technological University) (submittedVersion, cc-by-nc-nd)
Funders
National Institutes of Health (R15GM104846)
Topics
  • Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
  • Physical Sciences › Engineering › Ocean Engineering › Marine Biology and Environmental Chemistry
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Hydrogels: synthesis, properties, applications
Keywords
mussel foot proteins, bioadhesives, catechol, DOPA, biomimetic materials, catechol-functionalized polymers, adhesive hydrogels, self-healing materials, biomedical adhesives, antifouling coatings, interfacial adhesion

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review