胶原蛋白基生物功能材料制备方法研究进展

doi:10.16085/j.issn.1000-6613.2017-0969

摘要/Abstract

摘要： 胶原蛋白具有强亲水性、优异的生物相容性、弱抗原性和易加工成型等独特的功能特性，已成为最有前途的绿色可再生材料之一。为了克服天然胶原蛋白材料热稳定性差、抗水性差、机械强度低、易酶解和易污染等缺陷，通常采用共价交联法、静电纺丝法、自组装法和相分离法等方法对胶原蛋白进行加工处理。本文首先介绍了胶原蛋白基生物功能材料的4种方法的制备原理，描述了4种方法的研究现状，指出了4种方法各自的优点和缺点，然后比较了4种方法的制备工艺、制备材料的结构和功能差异，最后展望了胶原蛋白基生物功能材料的研究前景。结果表明：胶原蛋白基生物功能材料作为清洁可再生材料在智能纳米药物载体、微型生物反应器、传感器、人造光俘获系统等领域具有广阔的应用前景。

关键词: 蛋白质, 胶原蛋白, 复合材料, 纳米结构, 制备, 生物工程

Abstract: Collagen has become one of the most promising green renewable functional materials due to its strong hydrophilicity, excellent biocompatibility, weak antigenicity, and easy to be processed. In order to overcome the disadvantages of natural collagen material, such as poor thermal stability, poor water resistance, low mechanical strength, easy enzymolysis and easy pollution, the collagen is usually processed by covalent cross-linking, electrospinning, self-assembly and phase separation. Firstly, the principle of four kinds of preparation methods was introduced. The research status of the four preparation methods was described. The advantages and disadvantages of the four methods were pointed out. Then, the preparation process, structure and function difference of the four methods were compared. Finally, the prospect of collagen based biomaterials was reviewed. Results showed that as a clean and renewable material, collagen based biomaterials have broad application prospects in the fields of micro bioreactor, sensor, mart drug delivery system, and artificial light harvesting system.

Key words: protein, collagen, composites, nanostructure, preparation, biological engineering

中图分类号:

TQ93

王瑞瑞, 王鸿儒. 胶原蛋白基生物功能材料制备方法研究进展[J]. 化工进展, 2018, 37(02): 592-598.

WANG Ruirui, WANG Hongru. Research progress in preparation methods of collagen based biomaterials[J]. Chemical Industry and Engineering Progress, 2018, 37(02): 592-598.

参考文献

[1] ANJA M O, TANITA J B, MONIKA G, et al. Modification of extruded chicken collagen films by addition of co-gelling protein and sodium chloride[J]. Journal of Food Engineering, 2017, 207(3):46-55.
[2] OECHSLE A M, AKGUN D, KRAUSE F, et al. Microstructure and physical-chemical properties of chicken collagen[J]. Food Structure, 2016, 7(2):29-37.
[3] OECHSLE A M, WITTMANN X, GIBIS M, et al. Collagen entanglement influenced by the addition of acids[J]. Eur. Polym. J., 2014, 58(1):144-156.
[4] 李凤娟,林炜,程庆甦,等. 新型胶原基pH敏感水凝胶的制备及性能[J]. 化工进展, 2009, 28(3):441-444. LI F J, LIN W, CHENG Q S, et al. Synthesis and characterization of pH-sensitive collagen-based hydrogels[J]. Chemical Industry and Engineering Progress, 2009, 28(3):441-444.
[5] 刘洁,赵世玉,徐洲,等. 胶原在两种离子液体[BMIM]Cl和[BMIM]Ac中的溶解及再生结构比较[J]. 化工学报, 2015, 66(6):2196-2204. LIU J, ZHAO S Y, XU Z, et al. Comparison of dissolution and regeneration structure of collagen with two ionic liquids:[BMIM]Cl and[BMIM]Ac[J]. CIESC Journal, 2015, 66(6):2196-2204.
[6] LIU D, LIANG L, REGENSTEIN J M, et al. Extraction and characterization of pepsin-solubilised collagen from fins, scales, skins, bones and swim bladders of bighead carp(hypophthalmichthys nobilis)[J]. Food Chemistry, 2012, 133(4):1441-1448.
[7] GREEN E C. Collagen fibril assembly in the presence of carbon nano-fillers:a fundamental structure property relationship study[D]. Boston, Massachusetts:Northeastern University, 2015.
[8] JUS S, STACHEL I, SCHLOEGL W, et al. Cross-linking of collagen with laccases and tyrosinases[J]. Materials Science and Engineering C, 2011, 31(3):1068-1077.
[9] HOLMES R, KIRK S, TRONCI G, et al. Influence of telopeptides on the structural and physical properties of polymeric and monomeric acid-soluble type Ⅰ collagen[J]. Materials Science and Engineering C, 2017, 77(3):823-827.
[10] NEEL E, BOZEC L, KNOWLES J C, et al. Collagen-emerging collagen based therapies hit the patient[J]. Adv. Drug Deliv. Rev., 2013, 65(9):429-456.
[11] Morimoto K,KUNⅡ S, HAMANO K, et al. Preparation and structural analysis of actinidain-processed atelocollagen of yellowfin tuna[J]. Bioscience Biotechnology and Biochemistry, 2004, 68(4):861-867.
[12] SERGIO T, JOSE V A, MARIA J O, et al. Comparative performance of electrospun collagen nanofibers cross-linked by means of different methods[J]. Applied Materials & Interfaces, 2009, 1(1):218-223.
[13] CHARULATHA A, RAJARAM A. Influence of different crosslinking treatments on the physical properties of collagen membranes[J]. Biomaterials, 2003, 24(5):759-767.
[14] LI F, GRIFFITH M, LI Z, et al. Recruitment of multiple cell lines by collagen-synthetic copolymer matrices in corneal regeneration[J]. Biomaterials, 2005, 26(9):3093-3104.
[15] CHU C Y, DENG J, MAN Y, et al. Evaluation of nanohydroxyapaptite(nano-HA) coated epigallocatechin-3-gallate (EGCG) cross-linked collagen membranes[J]. Materials Science and Engineering C, 2017, 78(4):258-264.
[16] SIZELAND K H, BASIL J, M M, et al. Collagen orientation and leather strength for selected mammals[J]. Journal of Agricultural and Food Chemistry, 2013, 61(4):887-892.
[17] WALTERS B D, STEGEMANN J P. Strategies for directing the structure and function of three-dimensional collagen biomaterials across length scales[J]. Acta Biomater., 2014, 10(4):1488-1501.
[18] NA N, MARIE J D. Protein-based hydrogels derived from industrial byproducts containing collagen, keratin, zein and soy[J]. Waste and Biomass Valorization, 2017, 8(2):285-300.
[19] PUNITHA V, RAGHAVA R J, BALACHANDRAN U N. Biochemical and biophysical characterization of EDC treated rattus type Ⅰ collagen[J]. Process Biochemistry, 2013, 48(4):1059-1064.
[20] EUN YOUNG J, BONG-HYUK C, DOOYUP J, et al. Natural healing-inspired collagen-targeting surgical protein glue for accelerated scarless skin regeneration[J]. Biomaterials, 2017, 134(4):154-165.
[21] HUSSILA K, NIKHIL T, ALAN J B, et al. Microporous collagen spheres produced via thermally induced phase separation for tissue regeneration[J]. Acta Biomaterialia, 2010, 6(8):1158-1166.
[22] FAN L H, WU H, CAO M, et al. Enzymatic synthesis of collagen peptide-carboxymethylated chitosan copolymer and its characterization[J]. Reactive & Functional Polymers, 2014, 76(1):26-31.
[23] KUO Y C, HSUEH C H. Neuronal production from induced pluripotent stem cells in self-assembled collagen-hyaluronic acid-alginate microgel scaffolds with grafted GRGDSP/Ln5-P4[J]. Materials Science and Engineering C, 2017, 76(1):760-774.
[24] INES S, UWE S, THOMAS H, et al. Cross-linking of type Ⅰ collagen with microbial transglutaminase:identification of crosslinking sites[J]. Biomacromolecules, 2010, 11(9):698-705.
[25] TOBIAS H,GRETA F,MICHAEL R,et al.Enzyme-catalyzed protein crosslinking[J]. Appl. Microbiol. Biotechnol., 2013, 97(1):461-475.
[26] EVERAERTS F, TORRIANNI M, HENDRIKS M. Biomechanical properties of carbodimide crosslinked collagen:influence of the formation of ester crosslinks[J]. J. Biomed. Mater. Res. A, 2008, 85(4):547-555.
[27] USHA R, SREERAM K J, RAJARAM A. Stabilization of collagen with EDC/NHS in the presence of L-lysine:a comprehensive study[J]. Colloids and Surfaces B:Biointerfaces, 2012, 90(5):83-90.
[28] ZHAO L L, LI X, ZHAO J Q, et al. A novel smart injectable hydrogel prepared by microbial transglutaminase and human-like collagen:its characterization and biocompatibility[J]. Material Science and Engineering C, 2016, 68(4):317-326.
[29] ZEUGOLIS D I, PANENGAD P P, YEW E S Y, et al. An in situ and in vitro investigation for the transglutaminase potential in tissue engineering[J]. Journal of Biomedical Materials Research Part A, 2009, 92(4):1310-1320.
[30] XIAO Y, GE H Y, ZOU S Q, et al. Enzymatic synthesis of N-succinyl chitosan-collagen peptide copolymer and its characterization[J]. Carbohydrate Polymers, 2017, 166(2):45-54.
[31] LEE Y, BAE J W, LEE J W, et al. Enzyme-catalyzed in situ forming gelatin hydrogels as bioactive wound dressings:effects of fibroblast delivery on wound healing efficacy[J]. Journal of Materials Chemistry B, 2014, 44(2):7712-7718.
[32] KUO K C, LIN R Z, TIEN H W, et al. Bioengineering vascularized tissue constructs using an injectable cell-laden enzymatically crosslinked collagen hydrogel derived from dermal extracellular matrix[J]. Acta Biomaterialia, 2015, 27(9):151-166.
[33] YANET E C, VICTOR A, ELEAZAR L S, et al. Physicochemical properties of polycaprolactone/collagen/elastin nanofibers fabricated by electrospining[J]. Materials Science and Engineering C, 2017, 76(2):897-907.
[34] KWAK S, HAIDER A, GUPTA K C, et al. Micro/Nano multilayered scaffolds of PLGA and collagen by alternately electrospinning for bone tissue engineering[J]. Nanoscale Res. Lett., 2016, 11(6):323.
[35] WADE R J, BURDICK J A. Advances in nanofibrous scaffolds for biomedical applications:from electrospinning to self-assembly[J]. Science Direct, 2014, 9(2):722-742.
[36] LIN K, CHUA K N, CHRISTOPHERSON G T, et al. Reducing electrospun nanofiber diameter and variability using cationic amphiphiles[J]. Polymer, 2007, 48(21):6384-6394.
[37] JIN G, LEE S, KIM S H, et al. Bicomponent electrospinning to fabricate three-dimensional hydrogel-hybrid nanofibrous scaffolds with spatial fiber tortuosity[J]. Biomedical Microdevices, 2014, 16(6):793-804.
[38] 王瑞瑞, 王鸿儒. 胶原蛋白自组装生物功能材料的研究进展[J]. 化工进展, 2017, 36(6):2214-2221. WANG R R, WANG H R. Progress of research on collagen self-assembly biological functional materials[J]. Chemical Industry and Engineering Progress, 2017, 36(6):2214-2221.
[39] HWANG W, KIM B H, DANDU R, et al. Surface induced nanofiber growth by self-assembly of a silk-elastinlike protein polymer[J]. Langmuir, 2009, 25(21):12682-12686.
[40] AO H Y, XIE Y T, TAN H L, et al. Fabrication and in vitro evaluation of stable collagen/hyaluronic acid biomimetic multilayer on titanium coatings[J]. Journal of the Royal Society Interface, 2013, 70(10):1-9.
[41] SHIN K H, KIM J W, KOH Y H, et al. Novel self-assembly-induced 3D plotting for macro/nano-porous collagen scaffolds comprised of nanofibrous collagen filaments[J]. Materials Letters, 2015, 143(9):265-268.
[42] KESHAW H, THAPAR N, BURNS A J, et al. Microporous collagen spheres produced via thermally induced phase separation for tissue regeneration[J]. Acta Biomaterialia, 2010, 6(3):1158-1166.
[43] TAKAAKI A, MITSUGU T. Effects of proliferation and differentiation of mesenchymal stem cells on compressive mechanical behavior of collagen/β-TCP composite scaffold[J]. Science Direct, 2014, 39(3):218-230.