Impact of Grafting Density on the Self-Assembly and Hydrophilicity of Succinylated Collagen

Wenxin Wang; Feiyi Shu; Lingyu Pan; Shanshan Huang; Xiao Tu; Ping Li; Siman Li; Yuanyuan Li; Chengzhi Xu; Yang Sun; Juntao Zhang; Haibo Wang

Macromolecular Research, Vol.28, No.6, 636-643, June, 2020

DOI10.1007/s13233-020-8077-1 Export Citation

Impact of Grafting Density on the Self-Assembly and Hydrophilicity of Succinylated Collagen

Wenxin Wang, Feiyi Shu, Lingyu Pan, Shanshan Huang, Xiao Tu, Ping Li, Siman Li, Yuanyuan Li, Chengzhi Xu, Yang Sun¹, Juntao Zhang^†, and Haibo Wang^†

School of Chemical and Environmental Engineering, Wuhan Polytechnic University, Wuhan, Hubei, P. R. China
¹School of Chemical Engineering and Food Science, Hubei University of Arts and Science, Xiangyang, Hubei, P. R. China

E-mail:,

Modification of protein could give their new functionality but would affect their intrinsic property and activity. In this paper, a series of succinylated collagen (SCol(n/1)) (n≥1) were prepared by modification of collagen with succinic anhydride at different molar ratio to amino groups amount of collagen. The impact of grafting density on the intrinsic self-assembly and additional hydrophilicity of succinylated collagen was explored. The results revealed that excessive grafting density of succinylated collagen would improve their hydrophilicity but weaken their self-assembly property, although the triple helix of collagen could be reserved after succinylation. SCol(1/1) (grafting density of 17%) with self-assembly property and good hydrophilicity was chosen to compare with native collagen. Compared to native collagen, thermostability of SCol(1/1) decreased slightly, however, SCol(1/1) could form softer hydrogel, which was more favorable for the proliferation of NIH/3 T3. The present work would help us to further understand the importance of grafting density for the design of modified collagen with intrinsic self-assembly property and additional new functionality.

Keywords:collagen;succinylation;self-assembly;hydrophilicity

[References]

Brodsky B, Ramshaw JAM, Matrix Biol., 15, 545 (1997)
Shoulders MD, Raines RT, Annu. Rev. Biochem., 78, 929 (2009)
Li C, Tian H, Duan L, Tian Z, Li G, Int. J. Biol. Macromol., 57, 92 (2013)
Gomez-Guillen MC, Gimenez B, Lopez-Caballero ME, Montero MP, Food Hydrocolloids, 25, 1813 (2011)
Kołodziejska I, Sikorski ZE, Niecikowska C, Food Chem., 66, 153 (1999)
Sripriya R, Kumar R, Balaji S, Kumar MS, Sehgal PK, React. Funct. Polym., 71(1), 62 (2011)
Zhang J, Zou M, Zhang M, Wei B, Xu C, Xie D, Wang H, Food Biophys, 11, 380 (2016)
Zhang M, Ding C, Yang J, Lin S, Chen L, Huang L, Carbohydr. Polym., 137, 410 (2016)
Kim SH, Lee JH, Yun SY, Yoo JS, Jun CH, Chung KY, Suh H, Rapid Commun. Mass Sp., 14, 2125 (2000)
Zhang Z, Liu W, Li D, Li G, Biosci. Biotechnol. Biochem., 71, 2057 (2007)
Kumar R, Sripriya R, Balaji S, Kumar MS, Sehgal PK, J. Mol. Struct., 994, 117 (2011)
Birk DE, Trelstad RL, J. Cell Biol., 103, 231 (1996)
Fratzl P, Curr. Opin. Colloid Interface Sci., 8, 32 (2003)
Fratzl P, Misof K, Zizak I, Rapp G, Amenitsch H, Bernstorff S, J. Struct. Biol., 122(1-2), 119 (1998)
Scott JE, Thomlinson AM, J. Anat., 192, 391 (1998)
Svensson L, Aszodi A, Reinholt FP, Fassler R, Heinegard D, Oldberg A, J. Biol. Chem., 274, 9636 (1999)
Dupont-Gillain CC, Colloid Surf. B, 124, 87 (2014)
Zhang J, Wei B, He L, Xu C, Xie D, Paik KW, Wang H, Macromol. Res., 25(11), 1105 (2017)
Tu X, Chen X, Peng Y, Nan J, Wei B, He L, Xu C, Xu Y, Xie D, Zhang J, Wang H, Macromol. Res., 26, 1233 (2018)
Zou M, Yang H, Wang H, Wang H, Zhang J, Wei B, Zhang H, Xie D, Int. J. Biol. Macromol., 92, 1175 (2016)
Reddy GK, Enwemeka CS, Clin. Biochem., 29, 225 (1996)
Tronci G, Russell SJ, Wood DJ, J. Mater. Chem. B, 1, 3705 (2013)
Klapper MH, Klotz IM, Met. Enzymol., 25, 531 (1972)
Zhang J, Tu X, Wang W, Nan J, Wei B, Xu C, He L, Xu Y, Li S, Wang H, Int. J. Biol. Macromol., 128, 885 (2019)
Noitup P, Morrissey MT, Garnjanagoonchorn W, J. Food Biochem., 30, 547 (2006)
Yan M, Li B, Zhao X, Qin S, Food Hydrocolloids, 29, 199 (2012)
Yang YL, Kaufman LJ, Biophys. J., 96, 1566 (2009)
Ravichandran R, Islam MM, Alarcon EI, Samanta A, Wang S, Lundstrom P, Hilborn J, Griffith M, Phopase J, J. Mater. Chem. B, 4, 318 (2016)
Feng YB, Melacini G, Taulane JP, Goodman M, J. Am. Chem. Soc., 118(43), 10351 (1996)
Tian H, Chen Y, Ding C, Li G, Carbohydr. Polym., 89, 542 (2012)
Dawes H, Boyes S, Keene J, Heatherbell D, Am. J. Enol. Viticult., 45, 319 (1994)
Pelegrine D, Gasparetto C, LWT-Food Sci. Technol., 38, 77 (2005)
Makhatadze GI, Privalov PL, Adv. Protein Chem., 47, 307 (1995)
Finch A, Ledward DA, BBA-Protein Struct, 278, 433 (1972)
Zhang J, Sun Y, Zhao Y, Wei B, Xu C, He L, Oliveria CLP, Wang H, Soft Matter, 13, 9220 (2017)
Cassel JM, Biopolymers, 4, 989 (1966)
Cooper A, Biochem. J., 118, 355 (1970)
Leikin S, Rau DC, Parsegian VA, Nat. Struct. Biol., 2, 205 (1995)
Yu Z, Xu Q, Dong C, Lee SS, Gao L, Li Y, D'Ortenzio M, Wu J, Curr. Pharm. Des., 21, 4342

[1] Brodsky B, Ramshaw JAM, Matrix Biol., 15, 545 (1997)

[2] Shoulders MD, Raines RT, Annu. Rev. Biochem., 78, 929 (2009)

[3] Li C, Tian H, Duan L, Tian Z, Li G, Int. J. Biol. Macromol., 57, 92 (2013)

[4] Gomez-Guillen MC, Gimenez B, Lopez-Caballero ME, Montero MP, Food Hydrocolloids, 25, 1813 (2011)

[5] Kołodziejska I, Sikorski ZE, Niecikowska C, Food Chem., 66, 153 (1999)

[6] Sripriya R, Kumar R, Balaji S, Kumar MS, Sehgal PK, React. Funct. Polym., 71(1), 62 (2011)

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

[8] Zhang M, Ding C, Yang J, Lin S, Chen L, Huang L, Carbohydr. Polym., 137, 410 (2016)

[9] Kim SH, Lee JH, Yun SY, Yoo JS, Jun CH, Chung KY, Suh H, Rapid Commun. Mass Sp., 14, 2125 (2000)

[10] Zhang Z, Liu W, Li D, Li G, Biosci. Biotechnol. Biochem., 71, 2057 (2007)

[11] Kumar R, Sripriya R, Balaji S, Kumar MS, Sehgal PK, J. Mol. Struct., 994, 117 (2011)

[12] Birk DE, Trelstad RL, J. Cell Biol., 103, 231 (1996)

[13] Fratzl P, Curr. Opin. Colloid Interface Sci., 8, 32 (2003)

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

[15] Scott JE, Thomlinson AM, J. Anat., 192, 391 (1998)

[16] Svensson L, Aszodi A, Reinholt FP, Fassler R, Heinegard D, Oldberg A, J. Biol. Chem., 274, 9636 (1999)

[17] Dupont-Gillain CC, Colloid Surf. B, 124, 87 (2014)

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

[19] Tu X, Chen X, Peng Y, Nan J, Wei B, He L, Xu C, Xu Y, Xie D, Zhang J, Wang H, Macromol. Res., 26, 1233 (2018)

[20] Zou M, Yang H, Wang H, Wang H, Zhang J, Wei B, Zhang H, Xie D, Int. J. Biol. Macromol., 92, 1175 (2016)

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

[22] Tronci G, Russell SJ, Wood DJ, J. Mater. Chem. B, 1, 3705 (2013)

[23] Klapper MH, Klotz IM, Met. Enzymol., 25, 531 (1972)

[24] Zhang J, Tu X, Wang W, Nan J, Wei B, Xu C, He L, Xu Y, Li S, Wang H, Int. J. Biol. Macromol., 128, 885 (2019)

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

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

[27] Yang YL, Kaufman LJ, Biophys. J., 96, 1566 (2009)

[28] Ravichandran R, Islam MM, Alarcon EI, Samanta A, Wang S, Lundstrom P, Hilborn J, Griffith M, Phopase J, J. Mater. Chem. B, 4, 318 (2016)

[29] Feng YB, Melacini G, Taulane JP, Goodman M, J. Am. Chem. Soc., 118(43), 10351 (1996)

[30] Tian H, Chen Y, Ding C, Li G, Carbohydr. Polym., 89, 542 (2012)

[31] Dawes H, Boyes S, Keene J, Heatherbell D, Am. J. Enol. Viticult., 45, 319 (1994)

[32] Pelegrine D, Gasparetto C, LWT-Food Sci. Technol., 38, 77 (2005)

[33] Makhatadze GI, Privalov PL, Adv. Protein Chem., 47, 307 (1995)

[34] Finch A, Ledward DA, BBA-Protein Struct, 278, 433 (1972)

[35] Zhang J, Sun Y, Zhao Y, Wei B, Xu C, He L, Oliveria CLP, Wang H, Soft Matter, 13, 9220 (2017)

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

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

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

[39] Yu Z, Xu Q, Dong C, Lee SS, Gao L, Li Y, D'Ortenzio M, Wu J, Curr. Pharm. Des., 21, 4342