The fiber properties of modacrylic fibers with silk protein and spinning technology for blended knitting yarns are studied. By testing the fiber properties, fiber spinnability is analysed. Modacrylic fibers with silk ...The fiber properties of modacrylic fibers with silk protein and spinning technology for blended knitting yarns are studied. By testing the fiber properties, fiber spinnability is analysed. Modacrylic fibers with silk protein are brittle and have poor cohesion, so the key to process modacrylic fibers with silk protein lies in forming lap and sliver. During opening and carding, low speed is used to decrease fiber damage and the proper static resistant oil is applied to eliminate lapping fibers. Besides, the temperature and relative humidity have to be strictly controlled. The applications of modacrylic fibers with silk protein are also put forward.展开更多
Molecular weights of the silk fibroin were determined by polyacrylamide gel electrophoresis in the presence of so-didium dodecyl sulfate (SDS - PAGE): The silk fibroin molecule consisted of subunits a, b and c with mo...Molecular weights of the silk fibroin were determined by polyacrylamide gel electrophoresis in the presence of so-didium dodecyl sulfate (SDS - PAGE): The silk fibroin molecule consisted of subunits a, b and c with molecular weights of 280 kD, 230 kD and 25 kD respectively, of which the b subunit was composed of two subunits e and f with molecular weights of 130 kD and 125 kD, respec-tively, connected by disulfide bonds. The conformation of silk fibroin and subunits was determinated by Raman spectroscopy and Large angle X - ray diffraction) LAXS. The native silk fibroin only contained a - helix and random coil, but there were three conformation such as random - coil.a - helix and β - sheet in the silk fibroin dissolved in KSCN solution and frozen at - 20 °C. This suggested that KSCN solution and - 20°C freezing action could lead to the conformational transi-tion from random - coil and a - helix to P - sheet. The a subunit mainly existed in β - sheet conformation, in con-trast, the c subunit was展开更多
Silk extracted from the cocoon of silkworm has been used as textile materials for thousands of years.Recently,silk has been redefined as a protein-based biomaterial with great potential in biomedical applications owin...Silk extracted from the cocoon of silkworm has been used as textile materials for thousands of years.Recently,silk has been redefined as a protein-based biomaterial with great potential in biomedical applications owing to its excellent mechanical properties,biocompatibility,and biodegradability.With the advances in silk processing technologies,a broad range of intriguing silk-based functional biomaterials have been made and applied for various biomedical uses.However,most of these materials are based on natural silk proteins without chemical modification,leading to limited control of properties and functions(e.g.,biodegradability and bioactivity).A chemical toolbox for modifying the silk proteins is required to achieve versatile silk-based materials with precisely designed properties or functions for different applications.Furthermore,inspired by the traditional fine chemical industry based on synthetic chemistry,developing silk-based fine chemicals with special functions can significantly extend the applications of silk materials,particularly in biomedical fields.This review summarizes the recent progress on chemical modification of silk proteins,focusing on the methodologies and applications.We also discuss the challenges and opportunities of these chemically modified silk proteins.展开更多
Silk protein builds one of the strongest natural fibers based on its complex nanocomposite structures.However,the mechanical performance of silk protein,related to its molecular structure and packing is still elusive....Silk protein builds one of the strongest natural fibers based on its complex nanocomposite structures.However,the mechanical performance of silk protein,related to its molecular structure and packing is still elusive.In this study,we constructed an atomistic silk protein network model,which reproduces the extensive connection topology of silk protein with structure details of theβ-sheet crystallites and amorphous domains.With the silk protein network model,we investigated the structure evolution and stress distribution of silk protein under external loading.We found a pre-stretching treatment during the spinning process can improve the strength of silk protein.This treatment improves the properties of silk protein network,i.e.,increases the number of nodes and bridges,makes the nodes distributed homogeneously,and induces the bridges in the network well aligned to the loading direction,which is of great benefit to the mechanical performances of silk protein.Our study not only provides a realized atomistic model for silk protein network that well represents the structures and deformations of silk proteins under loading,but also gains deep insights into the mechanism how the pre-loading on silk proteins during spinning improves the mechanical properties of silk fibers.展开更多
The posterior silk gland （PSG） of silkworm is an important organ where fibroin is synthesized and secreted exclusively. Because fibroin constitutes 75-80% of the silk filament, the mechanism governing fibroin secret...The posterior silk gland （PSG） of silkworm is an important organ where fibroin is synthesized and secreted exclusively. Because fibroin constitutes 75-80% of the silk filament, the mechanism governing fibroin secretion, quality and yield of cocoon can be elucidated by the study on the PSG. Using two-dimensional gel electrophoresis （2-DE） and image analysis system, the changes in the protein composition in the PSG cell were investigated on the day 1 （D1） and day 4 （D4） in the 5th instar stage from five different strains of silkworm （Bombyx mori）. While differences at protein level between days and strains were far less than those observed at the gene level using EST analysis. The change trends in protein composition from D1 to D4 were diverse among the different strains. The results suggest that the secretion of fibroin is regulated by multiple proteins. The site of regulation and the proteins responsible for the regulation vary with the strain, which leads to differences between strains in the capacity of fibroin secretion in the PSG cell.展开更多
Zeolitic imidazolate frameworks(ZIFs)are an important subclass of metal-organic frameworks(MOFs)with zeolite-type topology,which can be fabricated under ambient synthesis conditions.However,the applications of ZIFs ar...Zeolitic imidazolate frameworks(ZIFs)are an important subclass of metal-organic frameworks(MOFs)with zeolite-type topology,which can be fabricated under ambient synthesis conditions.However,the applications of ZIFs are commonly limited due to the weak hydrostability of their metal–ligand coordination bonds,particularly under humid and aqueous conditions.In this work,as an example,the hydrolysis behaviours of ZIF-L with a special focus on ZIF-L coatings were tested at aqueous conditions with a wide range of pHs to systematically study and fundamentally understand their structural stability and degradation mechanism.Pristine ZIF-L powder and ZIF-L coatings were severely damaged after only 24 h in aqueous media.Interestingly,the ZIF-L coatings showed two distinct hydrolyzation pathways regardless of pH conditions,exhibiting either a ring-shaped etching or unfolding behaviours.While the ZIF-L powders were hydrolyzed almost identically across all pH conditions.With this new understanding,a facile silk fibroin(SF)protein modification method was developed to enhance the hydrostability of ZIF-L coatings in aqueous media.The effect of protein concentration on surface coating was systemically studied.ZIF-L coating retained its surface morphology after soaking in water and demonstrated switchable super wetting properties and superior separation performance for oil/water mixture.As a result,the quick SF protein modification significantly enhanced the stability of ZIF-L coatings under various pHs,while retaining their switchable wetting property and excellent separation performance.展开更多
丝素蛋白是一种从蚕丝中提取的天然高分子纤维蛋白,有很好的抗氧化和减少光损伤的作用。为了研究丝素蛋白对皮肤光损伤的保护作用,以UVB诱导人角质形成细胞(HaCaT)损伤为模型,通过ELISA和荧光检测细胞内活性氧(ROS)和钙离子(Ca^(2+))的...丝素蛋白是一种从蚕丝中提取的天然高分子纤维蛋白,有很好的抗氧化和减少光损伤的作用。为了研究丝素蛋白对皮肤光损伤的保护作用,以UVB诱导人角质形成细胞(HaCaT)损伤为模型,通过ELISA和荧光检测细胞内活性氧(ROS)和钙离子(Ca^(2+))的水平,采用免疫荧光检测瞬时受体电位阳离子通道亚家族V成员1(TRPV1)和Claudin-1的表达。此外,还使用蛋白质印迹分析了紧密连接相关蛋白Occludin和Claudin-1的表达。结果表明,120 m J/cm^(2)的UVB刺激显著降低细胞活力,而100μg/m L丝素蛋白的存在显著增加细胞活力。UVB刺激导致细胞内活性氧水平升高,激活TRPV1通道,诱导细胞内Ca^(2+)水平增加。同时炎症因子白细胞介素1α(IL-1α)(P<0.01)和S100钙结合蛋白A8(S100A8)(P<0.05)水平也显著升高,引发炎症反应。添加丝素蛋白的HaCaT细胞受到UVB的影响则显著降低(P<0.05)。实验证明,UVB会破坏屏障蛋白,导致屏障蛋白Claudin-1和Occludin的表达下降。丝素蛋白的加入可以降低这种影响,保护细胞间紧密连接。因此,丝素蛋白可能具有降低氧化应激、屏障损伤和炎症发生,保护皮肤免受UVB诱导的光损伤的潜在能力。展开更多
文摘The fiber properties of modacrylic fibers with silk protein and spinning technology for blended knitting yarns are studied. By testing the fiber properties, fiber spinnability is analysed. Modacrylic fibers with silk protein are brittle and have poor cohesion, so the key to process modacrylic fibers with silk protein lies in forming lap and sliver. During opening and carding, low speed is used to decrease fiber damage and the proper static resistant oil is applied to eliminate lapping fibers. Besides, the temperature and relative humidity have to be strictly controlled. The applications of modacrylic fibers with silk protein are also put forward.
基金the Foundation of Hao Yingdong Youth Teacher and Shanghai Youth Scientific
文摘Molecular weights of the silk fibroin were determined by polyacrylamide gel electrophoresis in the presence of so-didium dodecyl sulfate (SDS - PAGE): The silk fibroin molecule consisted of subunits a, b and c with molecular weights of 280 kD, 230 kD and 25 kD respectively, of which the b subunit was composed of two subunits e and f with molecular weights of 130 kD and 125 kD, respec-tively, connected by disulfide bonds. The conformation of silk fibroin and subunits was determinated by Raman spectroscopy and Large angle X - ray diffraction) LAXS. The native silk fibroin only contained a - helix and random coil, but there were three conformation such as random - coil.a - helix and β - sheet in the silk fibroin dissolved in KSCN solution and frozen at - 20 °C. This suggested that KSCN solution and - 20°C freezing action could lead to the conformational transi-tion from random - coil and a - helix to P - sheet. The a subunit mainly existed in β - sheet conformation, in con-trast, the c subunit was
基金This work was supported by National Natural Science Foundation of China(No.52103129)Foundation of Westlake University.
文摘Silk extracted from the cocoon of silkworm has been used as textile materials for thousands of years.Recently,silk has been redefined as a protein-based biomaterial with great potential in biomedical applications owing to its excellent mechanical properties,biocompatibility,and biodegradability.With the advances in silk processing technologies,a broad range of intriguing silk-based functional biomaterials have been made and applied for various biomedical uses.However,most of these materials are based on natural silk proteins without chemical modification,leading to limited control of properties and functions(e.g.,biodegradability and bioactivity).A chemical toolbox for modifying the silk proteins is required to achieve versatile silk-based materials with precisely designed properties or functions for different applications.Furthermore,inspired by the traditional fine chemical industry based on synthetic chemistry,developing silk-based fine chemicals with special functions can significantly extend the applications of silk materials,particularly in biomedical fields.This review summarizes the recent progress on chemical modification of silk proteins,focusing on the methodologies and applications.We also discuss the challenges and opportunities of these chemically modified silk proteins.
基金This work was supported by the National Natural Science Foundation of China(Grants Nos.12122212,11932017,11772054,and 11772055).
文摘Silk protein builds one of the strongest natural fibers based on its complex nanocomposite structures.However,the mechanical performance of silk protein,related to its molecular structure and packing is still elusive.In this study,we constructed an atomistic silk protein network model,which reproduces the extensive connection topology of silk protein with structure details of theβ-sheet crystallites and amorphous domains.With the silk protein network model,we investigated the structure evolution and stress distribution of silk protein under external loading.We found a pre-stretching treatment during the spinning process can improve the strength of silk protein.This treatment improves the properties of silk protein network,i.e.,increases the number of nodes and bridges,makes the nodes distributed homogeneously,and induces the bridges in the network well aligned to the loading direction,which is of great benefit to the mechanical performances of silk protein.Our study not only provides a realized atomistic model for silk protein network that well represents the structures and deformations of silk proteins under loading,but also gains deep insights into the mechanism how the pre-loading on silk proteins during spinning improves the mechanical properties of silk fibers.
文摘The posterior silk gland （PSG） of silkworm is an important organ where fibroin is synthesized and secreted exclusively. Because fibroin constitutes 75-80% of the silk filament, the mechanism governing fibroin secretion, quality and yield of cocoon can be elucidated by the study on the PSG. Using two-dimensional gel electrophoresis （2-DE） and image analysis system, the changes in the protein composition in the PSG cell were investigated on the day 1 （D1） and day 4 （D4） in the 5th instar stage from five different strains of silkworm （Bombyx mori）. While differences at protein level between days and strains were far less than those observed at the gene level using EST analysis. The change trends in protein composition from D1 to D4 were diverse among the different strains. The results suggest that the secretion of fibroin is regulated by multiple proteins. The site of regulation and the proteins responsible for the regulation vary with the strain, which leads to differences between strains in the capacity of fibroin secretion in the PSG cell.
基金supported by start-up funding from the School of Engineering,at the University of Edinburgh.
文摘Zeolitic imidazolate frameworks(ZIFs)are an important subclass of metal-organic frameworks(MOFs)with zeolite-type topology,which can be fabricated under ambient synthesis conditions.However,the applications of ZIFs are commonly limited due to the weak hydrostability of their metal–ligand coordination bonds,particularly under humid and aqueous conditions.In this work,as an example,the hydrolysis behaviours of ZIF-L with a special focus on ZIF-L coatings were tested at aqueous conditions with a wide range of pHs to systematically study and fundamentally understand their structural stability and degradation mechanism.Pristine ZIF-L powder and ZIF-L coatings were severely damaged after only 24 h in aqueous media.Interestingly,the ZIF-L coatings showed two distinct hydrolyzation pathways regardless of pH conditions,exhibiting either a ring-shaped etching or unfolding behaviours.While the ZIF-L powders were hydrolyzed almost identically across all pH conditions.With this new understanding,a facile silk fibroin(SF)protein modification method was developed to enhance the hydrostability of ZIF-L coatings in aqueous media.The effect of protein concentration on surface coating was systemically studied.ZIF-L coating retained its surface morphology after soaking in water and demonstrated switchable super wetting properties and superior separation performance for oil/water mixture.As a result,the quick SF protein modification significantly enhanced the stability of ZIF-L coatings under various pHs,while retaining their switchable wetting property and excellent separation performance.
文摘丝素蛋白是一种从蚕丝中提取的天然高分子纤维蛋白,有很好的抗氧化和减少光损伤的作用。为了研究丝素蛋白对皮肤光损伤的保护作用,以UVB诱导人角质形成细胞(HaCaT)损伤为模型,通过ELISA和荧光检测细胞内活性氧(ROS)和钙离子(Ca^(2+))的水平,采用免疫荧光检测瞬时受体电位阳离子通道亚家族V成员1(TRPV1)和Claudin-1的表达。此外,还使用蛋白质印迹分析了紧密连接相关蛋白Occludin和Claudin-1的表达。结果表明,120 m J/cm^(2)的UVB刺激显著降低细胞活力,而100μg/m L丝素蛋白的存在显著增加细胞活力。UVB刺激导致细胞内活性氧水平升高,激活TRPV1通道,诱导细胞内Ca^(2+)水平增加。同时炎症因子白细胞介素1α(IL-1α)(P<0.01)和S100钙结合蛋白A8(S100A8)(P<0.05)水平也显著升高,引发炎症反应。添加丝素蛋白的HaCaT细胞受到UVB的影响则显著降低(P<0.05)。实验证明,UVB会破坏屏障蛋白,导致屏障蛋白Claudin-1和Occludin的表达下降。丝素蛋白的加入可以降低这种影响,保护细胞间紧密连接。因此,丝素蛋白可能具有降低氧化应激、屏障损伤和炎症发生,保护皮肤免受UVB诱导的光损伤的潜在能力。
