Molecular Aggregation Behavior and Biological Properties of Regenerated Silk Fibroin in Na<sup>+</sup> Solution

YING Yong; WANG Yunxuan; GUO Lei; XU Yuling; ZHANG Juntao; XU Chengzhi; WEI Benmei; WANG Haibo

doi:10.13386/j.issn1002-0306.2023090155

Volume 45 Issue 17

Aug. 2024

Turn off MathJax

Article Contents

Abstract

References

Supplements

Science and Technology of Food Industry > 2024 > 45(17): 65-72. > DOI: 10.13386/j.issn1002-0306.2023090155

YING Yong, WANG Yunxuan, GUO Lei, et al. Molecular Aggregation Behavior and Biological Properties of Regenerated Silk Fibroin in Na⁺ Solution[J]. Science and Technology of Food Industry, 2024, 45(17): 65−72. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2023090155.

Citation:

PDF (2790 KB)

Molecular Aggregation Behavior and Biological Properties of Regenerated Silk Fibroin in Na⁺ Solution

1.
School of Chemical & Environmental Engineering, Wuhan Polytechnic University, Wuhan 430023, China
2.
College of Life Science and Technology, Hubei Key Laboratory of Quality Control of Characteristic Fruits and Vegetables, Hubei Engineering University, Xiaogan 432000, China

More Information

Received Date: September 13, 2023
Available Online: June 30, 2024

Graphical Abstract

Abstract

Abstract

Objective: The aggregation behavior of silk fibroin under specific conditions can influence its kinetic behavior and viscoelastic properties, thereby affecting biological properties of silk fibroin materials. Therefore, this study systematically investigated the self-assembly aggregation behavior of silk fibroin and explored the conditions for enhancing its mechanical performance and biological properties. Methods: Regenerated silk fibroin was extracted and prepared from domestic silkworm cocoons, and the optimal assembly conditions were determined through turbidity experiments. Rheological experiments were conducted to study the influence of Na⁺ on the kinetic behavior and viscoelastic properties of silk fibroin solutions. Cell proliferation experiments were carried out to investigate the biological properties of silk fibroin. Results: The extracted regenerated silk fibroin primarily exhibited a random coiled structure. The optimal in vitro self-assembly conditions involved assembly of a 4 mg/mL solution at 70 ℃ for 6 hours. The addition of Ca²⁺ to the silk fibroin solution inhibited in vitro self-assembly, while the addition of Na⁺ accelerated the assembly rate and increased the degree of assembly. Furthermore, with increasing Na⁺ concentration, the gel strength of silk fibroin gradually increased, leading to a more stable gel network. Cell proliferation experiments demonstrated that the solution of regenerated silk fibroin was more conducive to cell growth and proliferation than its self-assembled fibers. Conclusion: The concentration, temperature, assembly time, and ions all have an impact on the in vitro self-assembly aggregation behavior of silk fibroin. This study provides preliminary research on the self-assembly aggregation conditions and biological properties of silk fibroin, offering experimental basis for improving the performance of silk fibroin as a food packaging material.
- regenerated silk fibroin,
- self assembly,
- rheology,
- viscoelasticity,
- assembly level

FullText(HTML)

References (36)

References

[1]	ARANGO M C, MONTOYA Y, PERESIN M S, et al. Silk sericin as a biomaterial for tissue engineering:A review[J]. International Journal of Polymeric Materials,2021,70(15/18):1115−1129.
[2]	CHELAZZI D, BADILLO-SANCHEZ D, GIORGI R, et al. Self-regenerated silk fibroin with controlled crystallinity for the reinforcement of silk[J]. Journal of Colloid and Interface Science,2020,576:230−240. doi: 10.1016/j.jcis.2020.04.114
[3]	MARELLI B, BRENCKLE M A, KAPLAN D L, et al. Silk fibroin as edible coating for perishable food preservation[J]. Scientific Reports,2016,6:25236. doi: 10.1038/srep25236
[4]	LIM H R, KIM H S, QAZI R, et al. Advanced soft materials, sensor integrations, and applications of wearable flexible hybrid electronics in healthcare, energy, and environment[J]. Advanced Materials,2020,32:1901924.1−1901924.43.
[5]	ZHANG X H, SHENG N N, WANG L A, et al. Supramolecular nanofibrillar hydrogels as highly stretchable, elastic and sensitive ionic sensors[J]. Materials Horizons Journal,2019,6:326−333. doi: 10.1039/C8MH01188E
[6]	WANG F, LIU H, LI Y Y, et al. Tunable biodegradable polylactide-SF fibroin scaffolds fabricated by a solvent-free pressure-controllable foaming technology[J]. ACS Applied Bio Materials,2020,3(12):8795−8807. doi: 10.1021/acsabm.0c01157
[7]	LIU S H, ZHANG H G, HU Q X, et al. Development and evaluation of biomimetic 3D coated composite scaffold for application as skin substitutes[J]. Macromolecular Materials and Engineering,2020,305(3):1900848.1−13.
[8]	CHENG G T, WANG X, SONG C X, et al. Directly self-assembling method to easily prepare rough silk fibroin film[J]. Soft Materials,2023,20(3):251−258.
[9]	FAN L P, LI J L, CAI Z X, et al. Bioactive hierarchical silk fibers created by bioinspired self-assembly[J]. Nature Communications,2021,12(1):2375−1384. doi: 10.1038/s41467-021-22673-4
[10]	PIRES M M, PRZYBYLA D E, PEREZ C M R, et al. Metalmediated tandem coassembly of collagen peptides into banded microstructures[J]. J Am Chem Soc,2011,133:14469−14471. doi: 10.1021/ja2042645
[11]	PRIYANKA D, SINCHAN S, PRAMIT K, et al. Effect of macromolecular crowders on the self-assembly process of silk fibroin[J]. Macromol Chem Phys,2020,221(16):2000113−2000122. doi: 10.1002/macp.202000113
[12]	PRZYBYLA D E, RUBERTT P C M, GLATON J, et al. Hierarchical assembly of collagen peptide triple helices into curved disks and metal ion-promoted hollow spheres[J]. J Am Chem Soc,2013,135:3418−3422. doi: 10.1021/ja307651e
[13]	GUO X, LIN N, LU S, et al. Preparation and biocompatibility characterization of silk fibroin 3D scaffolds[J]. ACS Applied Bio Materials,2022,4(2):1369−1380.
[14]	CHEN F, LU S P, ZHU L, et al. Conductive regenerated silk fibroin-based hydrogels with integrated high mechanical performances[J]. J Mater Chem B,2019,7:1708−1715. doi: 10.1039/C8TB02445F
[15]	BAI Y, LUO Q, ZHANG W, et al. Highly ordered protein nanorings designed by accurate control of glutathione S-transferase self-assembly[J]. Jam Chem Soc,2013,135:10966−10969. doi: 10.1021/ja405519s
[16]	PERERA D, LI L X, WALSH C, et al. Natural spider silk nanofibrils produced by assembling molecules or disassembling fibers[J]. Acta Biomaterialia,2023,168:323−332. doi: 10.1016/j.actbio.2023.06.044
[17]	CHEN N, LIN L, SUN W, et al. Stable and pH-sensitive protein nanogels made by self-assembly of heat denatured soy protein[J]. J Agr Food Chem,2014,62:9553−9561. doi: 10.1021/jf502572d
[18]	PARAMONOV S E, JUN H W, HARTGERINK J D. Self-assembly of peptide-amphiphile nanofibers:The roles of hydrogen bonding and amphiphilic packing[J]. J Am Chem Soc,2006,128:7291−7298. doi: 10.1021/ja060573x
[19]	WILLIAMS R J, MART R J, ULIJN R V. Exploiting biocatalysis in peptide self-assembly peptide[J]. Science,2010,94:107−117.
[20]	PAGEL K, SERI T, VON B H, et al. How metal ions affect amyloid formation:Cu²⁺ and Zn²⁺ sensitive peptides[J]. Chem Bio Chem,2008,9:531−536. doi: 10.1002/cbic.200700656
[21]	LI W H, SU X P, ZHONG Q W, et al. Influence of reaction conditions on the self-assembly of the natural silk sericin protein[J]. Microsc Res Tech,2017,80(3):298−304. doi: 10.1002/jemt.22666
[22]	ZHANG Y H, JIANG T, ZHENG Y W, et al. Interference of EGCG on the Zn(II)-induced conformational transition of silk fibroin as a model protein related to neurodegenerative diseases[J]. Soft Matter,2012,8:5543−5549. doi: 10.1039/c2sm25099c
[23]	刘章会, 刘燕, 陈媛媛, 等. 丝素蛋白纳米颗粒的制备及其在食品领域的应用[J]. 食品与发酵工业, 2024, 50(14): 334-341. [LIU Z H, LIU Y, CHEN Y Y, et al. Preparation of silk fibroin nanoparticles and its application in food field: A review[J]. Food and Fermentation Industries, 2024, 50(14): 334-341.] LIU Z H, LIU Y, CHEN Y Y, et al. Preparation of silk fibroin nanoparticles and its application in food field: A review[J]. Food and Fermentation Industries, 2024, 50(14): 334-341.
[24]	LI F, WANG X, CHEN L, et al. Efficient development of silk fibroin membranes on liquid surface for potential use in biomedical materials[J]. International Journal of Biological Macromolecules:Structure, Function and Interactions,2021,182(Pt.1):237−243.
[25]	XIAO Y L, LIU Y W, ZHANG W W, et al. Formation, structure, and mechanical performance of silk nanofibrils produced by heat-induced self-assembly[J]. Macromol Rapid Commun,2020,42(3):e2000435.
[26]	DOU H, ZUO B Q. Effect of sodium carbonate concentrations on the degumming and regeneration process of silk fibroin[J]. The Journal of The Textile Institute, 2015, 106(3):311−319.
[27]	BATH J D, ELLIS J W. Some features and implications of the near infrared absorption spectra of various proteins:Gelatin, silk fibroin, and zinc insulinate[J]. J Phys Chem, 2002, 45(2):204−209.
[28]	XU Y L, DAI L, LI K, et al. Ground type-I collagen-A focused study on its fibrillogenesis behavior and bioactivity in vitro[J]. Macromolecular Research,2023,31(1):75−83. doi: 10.1007/s13233-022-00108-3
[29]	MOBINI S, HOYER B, HASHJIN M S, et al. Fabrication and characterization of regenerated silk scaffolds reinforced with natural silk fibers for bone tissue engineering[J]. Journal of Biomedical Materials Research Part A,2013,101(8):2392−2404.
[30]	NOITUP P, MORRISSEYORRISSE M T, GARNJANAGOONCHORN W. In vitro self-assembly of silver-line grunt type Ⅰ collagen:Effects of collagen concentrations, pH and temperatures on collagen self-assembly[J]. Journal of Food Biochemistry,2006,30(5):547−555. doi: 10.1111/j.1745-4514.2006.00081.x
[31]	LEE N R, BOWERMAN C J, NILSSON B L. Effects of varied sequence pattern on the self-assembly of amphipathic peptides[J]. Biomacromolecules,2013,14:3267−3277. doi: 10.1021/bm400876s
[32]	LIU Z G, CAI Y R, JIA Y R, et al. One-step synthesis of natural silk sericin-based microcapsules with bionic[J]. Structures Macromol Rapid Commun,2014,35(19):1668−1672. doi: 10.1002/marc.201400304
[33]	WANG J, ZHANG S S, XING T L, et al. Ion-induced fabrication of silk fibroin nanoparticles from Chinese oak tasar Antheraea pernyi[J]. International Journal of Biological Macromolecules,2015,79:316−325. doi: 10.1016/j.ijbiomac.2015.04.052
[34]	HORAN R L, ANTLE K, COLLETTE A L, et al. In vitro degradation of silk fibroin[J]. Biomaterials,2005,26(17):3385−3393. doi: 10.1016/j.biomaterials.2004.09.020
[35]	PRIPATNANONT P, CHANKUM C, MEESANE J, et al. Physical and biological performances of a semi-resorbable barrier membrane based on silk fibroin-glycerol-fish collagen material for guided bone regeneration[J]. Journal of Biomaterials Applications,2021,36(5):930−942. doi: 10.1177/08853282211025781
[36]	WEI J, IGARASHI T, OKUMORI N, et al. Influence of surface wettability on competitive protein adsorption and initial attachment of osteoblasts[J]. Biomed Mater,2009,4:045002−045008. doi: 10.1088/1748-6041/4/4/045002

[1]	JIANG Xiujie, ZHANG Jiayu, LI Ying, CHI Xiaoxing, SUN Dongbo, CAO Dongmei, ZHANG Dongjie. Effect of Rich GABA of Germinated Adzuki Bean on Intestinal Microflora in T2DM Mice[J]. Science and Technology of Food Industry, 2024, 45(12): 151-159. DOI: 10.13386/j.issn1002-0306.2023120301
[2]	CHENG Xiaoyang, LIAO Ming, HE Quanguang, MO Caifeng, HUANG Maokang, HUANG Meihua. Effects of Tetrastigma hemsleyanum Superfine Powder on Intestinal Microflora in Rats with Alcohol-Induced Liver Injury[J]. Science and Technology of Food Industry, 2023, 44(18): 415-424. DOI: 10.13386/j.issn1002-0306.2022090022
[3]	MU Rui, XIA Yunshi, ZHANG Yanting, BO Panpan, SUN Yinshi, WANG Zhitong, HUA Mei. Research Progress on the Chemical Composition and Intestinal Flora Regulation of Dietary Fiber from the Edible and Medicinal Plants[J]. Science and Technology of Food Industry, 2022, 43(18): 493-500. DOI: 10.13386/j.issn1002-0306.2021090216
[4]	ZHANG Zhixuan, HAN Jiaojiao, BAO Wei, WANG Ziyan, LIU Yan, HUO Chunheng, SU Xiurong. Regulation of Fermented Wax Gourd on Intestinal Microflora of Mice Infected with Staphylococcus aureus[J]. Science and Technology of Food Industry, 2021, 42(20): 149-156. DOI: 10.13386/j.issn1002-0306.2021040128
[5]	QI Yan, ZHOU Yan, ZHANG Xu-dong, WU Chun-zhen, TAn Jun, CHEN Dai-jie. Effect of Selenium-enriched Bifidobacterium longum DD98 on Diarrhea and Intestinal Microflora in Diarrhea Mice Induced by Irinotecan[J]. Science and Technology of Food Industry, 2020, 41(6): 292-298. DOI: 10.13386/j.issn1002-0306.2020.06.049
[6]	WANG Wen-ning, ZHANG Xiao-feng, HAN Ping, YU Fei, CAO Yang. Effects of Turnip on Intestinal Flora of Mice[J]. Science and Technology of Food Industry, 2018, 39(14): 287-291. DOI: 10.13386/j.issn1002-0306.2018.14.054
[7]	LI Jing, LV Xiao-ling, LV Dong-xue, WANG Meng-shu, ZHAO Sheng-nan, ZHAO Huan-jiao. Establishment of mice model for intestinal dysbacteria induced by cefixime dispersible tablets[J]. Science and Technology of Food Industry, 2017, (05): 361-365. DOI: 10.13386/j.issn1002-0306.2017.05.060
[8]	FU Jiao-jiao, PENG Zhi-yun, LIU Hai-quan, SUN Xiao-hong, PAN Ying-jie, ZHAO Yong. Changes of acidic electrolyzed water on intestinal microflora diversity of Penaeus vannawei during storage[J]. Science and Technology of Food Industry, 2015, (04): 344-347. DOI: 10.13386/j.issn1002-0306.2015.04.066
[9]	JIN Zhi-min, ZHANG Hong-bo, LIU Xia-wei, WANG Bo-hui, LUO Yu-long, YUAN Qian, DUAN Yan, TIAN Jian-jun, JIN Ye. Effects of supplementation of Lactobacillus plantarum with different dosage on fecal microbiota[J]. Science and Technology of Food Industry, 2014, (24): 342-345. DOI: 10.13386/j.issn1002-0306.2014.24.064
[10]	LIU Yun, LV Jiao, REN Wen-jin, Chen Hou-rong, LIU Xiong. Effect of the non-volatile parts of Zanthoxylum essential oil on intestinal health in rats[J]. Science and Technology of Food Industry, 2014, (09): 338-342. DOI: 10.13386/j.issn1002-0306.2014.09.065