Modulation of the Self-Assembly of Collagen by Phytic Acid: An In Vitro Study

Xiao Tu; Xincheng Chen; Ying Peng; Jie Nan; Benmei Wei; Lang He; Chengzhi Xu; Yuling Xu; Dong Xie; Juntao Zhang; Haibo Wang

Macromolecular Research, Vol.26, No.13, 1233-1240, December, 2018

DOI10.1007/s13233-019-7016-5 Export Citation

Modulation of the Self-Assembly of Collagen by Phytic Acid: An In Vitro Study

Xiao Tu, Xincheng Chen, Ying Peng, Jie Nan, Benmei Wei, Lang He, Chengzhi Xu, Yuling Xu, Dong Xie, Juntao Zhang^†, and Haibo Wang^†

School of Chemical and Environmental Engineering, Wuhan Polytechnic University, Wuhan, Hubei, 430023, P. R. China

E-mail:,

Phytic acid, containing a myoinositol ring coupled with six phosphate groups, can react with the amino groups of collagen to regulate their self-assembly behavior. The aim of this research is to evaluate the effects of phytic acid on the selfassembly behavior of collagen, the structures and properties of the resulting fibrils and hydrogels. Turbidity and chloramine T assay suggested that phytic acid could improve the self-assembly kinetics and degree of collagen, and the optimal ratio of phytic acid/collagen was 1/1 (w/w). Scanning electron microscopy (SEM) analysis indicated that co-fibrils of collagen with phytic acid are more slender than that of pure collagen, and transmission electron microscopy (TEM) reveals that the characteristic D-periodicity of collagen fibrils is not affected by phytic acid. Besides, differential scanning calorimetry (DSC) and rheology revealed that the thermal stability of collagen fibrils and the viscoelasticity of collagen hydrogels could be improved by phytic acid and the optimal ratio of phytic acid/collagen is 1/1 (w/w).

Keywords:collagen;phytic acid;self-assembly;kinetics;structure;property

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[Referenced By]

[1] Pati F, Adhikari B, Dhara S, Bioresour. Technol., 101(10), 3737 (2010)

[2] Traub W, Piez KA, Adv. Protein Chem., 25, 243 (1971)

[3] Eastoe JE, Biochem. J., 61, 589 (1955)

[4] Zhang J, Zou M, Zhang M, Wei B, Xu C, Xie D, Wang H, Food Biophys, 11, 380 (2016)

[5] Lee SJ, Liu J, Oh SH, Soker S, Atala A, Yoo JJ, Biomaterials, 29, 2891 (2008)

[6] Akturk O, Tezcaner A, Bilgili H, Deveci MS, Gecit MR, Keskin D, J. Biosci. Bioeng., 112(3), 279 (2011)

[7] Chung C, Burdick JA, Adv. Drug Deliv. Rev., 60, 243 (2008)

[8] Baik SH, Kim JH, Cho HH, Park S, Kim YS, Suh H, J. Surg. Res., 164, 221 (2010)

[9] Fratzl P, Weinkamer R, Prog. Mater. Sci., 52(8), 1263 (2007)

[10] Fratzl P, Misof K, Zizak I, Rapp G, Amenitsch H, Bernstorff S, J. Struct. Biol., 122(1-2), 119 (1998)

[11] Lynn AK, Yannas IV, Bonfield W, J. Biomed. Mater. Res. B, 71, 343 (2004)

[12] Fratzl P, Collagen: Structure and Mechanics, Springer Science + Business Media, New York, 2008.

[13] Fang M, Goldstein EL, Matich EK, Orr BG, Holl MMB, Langmuir, 29(7), 2330 (2013)

[14] Pins GD, Silver FH, Mater. Sci. Eng. C-Biomimetic Supramol. Syst., 3, 101 (1995)

[15] Zhang J, Wei B, He L, Xu C, Xie D, Paik KW, Wang H, Macromol. Res., 25(11), 1105 (2017)

[16] Zhang M, Wu K, Li G, Int. J. Biol. Macromol., 49, 847 (2011)

[17] Zhai Z, Wang H, Wei B, Yu P, Xu C, He L, Zhang J, Xu Y, Macromol. Res., 26(7), 609 (2018)

[18] Gough JE, Scotchford CA, Downes S, J. Biomed. Mater. Res. Part A, 61, 121 (2002)

[19] Febles CI, Arias A, Hardisson A, Rodriguez-Alvarez C, Sierra A, J. Cereal Sci., 36, 19 (2002)

[20] Ravichandran R, Seitz V, Venugopal JR, Sridhar R, Sundarrajan S, Mukherjee S, Wintermantel E, Ramakrishna S, Macromol. Biosci., 13, 366 (2013)

[21] Dost K, Tokul O, Anal. Chim. Acta, 558, 22 (2006)

[22] Graf E, Empson KL, Eaton JW, J. Biol. Chem., 262, 11647 (1987)

[23] Wang X, Wen K, Yang X, Li L, Yu X, J. Mater. Chem. B, 5, 8115 (2017)

[24] Yan M, Li B, Zhao X, Qin S, Food Hydrocolloids, 29, 199 (2012)

[25] Bae I, Osatom K, Yoshida A, Yamaguchi A, Tachibana K, Oda T, Hara K, Fisheries Sci., 75, 765 (2009)

[26] Reddy GK, Enwemeka CS, Clin. Biochem., 29, 225 (1996)

[27] Noitup P, Morrissey MT, Garnjanagoonchorn W, J. Food Biochem., 30, 547 (2006)

[28] Cooper A, Biochem. J., 118, 355 (1970)

[29] Cassel JM, Biopolymers, 4, 989 (1966)

[30] Leikin S, Rau DC, Parsegian VA, Nat. Struct. Biol., 2, 205 (1995)

[31] Mu C, Li D, Lin W, Ding Y, Zhang G, Biopolymers, 86, 282 (2007)

[32] Usha R, Jaimohan SM, Rajaram A, Mandal AB, Int. J. Biol. Macromol., 47, 402 (2010)

[33] Ding C, Zhang M, Tian H, Li G, Int. J. Biol. Macromol., 52, 319 (2013)

[34] Cheng X, Gurkan UA, Dehen CJ, Tate MP, Hillhouse HW, Simpson GJ, Akkus O, Biomaterials, 29, 3278 (2008)

[35] Li Y, Asadi A, Margo RM, Elliot PD, Mater. Sci. Eng. C-Biomimetic Supramol. Syst., 29, 1643 (2009)

[36] Tian H, Li C, Liu W, Li J, Li G, Colloids Surf. B: Biointerfaces, 105, 259 (2013)

[37] Velegol D, Lanni F, Biophys. J., 81, 1786 (2001)