CN110886092B - 蚕丝蛋白环境刺激响应致动器件的制备方法及使用方法 - Google Patents
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Abstract
本发明公开一种蚕丝蛋白环境刺激响应致动器件的制备方法及使用方法。本发明通过将蚕丝在低共熔深度溶剂中处理,制备得到具有微米以及纳米尺度的纤丝,通过控制制备条件使纤丝产生新的表面微观形貌和结构变化;进而将纤丝自组装为膜状器件,利用纤丝的选择性吸附和透过性能,通过控制器件两侧环境如温度、湿度以及环境中气体的不同以实现折叠、弯曲、支撑等运动行为。本发明在环境响应、人工智能等领域具有广泛的应用前景。
Description
技术领域
本发明涉及一种蚕丝蛋白环境刺激响应致动器件的制备方法及使用方法,所制备的材料具有极佳湿敏性、强度等可用于纳米机器人、传感器等领域。
背景技术
丝蛋白是由家蚕生产的天然高分子蛋白,丝蛋白由丝素和丝胶两种蛋白组成,通常丝素占74%而丝胶约占24%。丝素蛋白具有可与胶原蛋白相媲美的良好的生物相容性;良好的细胞附着性,且具有维持细胞正常形态,不影响细胞活性的功能;对机体无致敏性、无毒害和刺激作用;可部分生物降解,并且其降解产物本身对组织无毒副作用。而蚕丝纤维是最强的弹性体天然生物材料之一,具有超强的、可扩展的和坚韧的特性。典型的纳米纤维结构由无定形链连接的纳米β-微晶组成,赋予蚕丝非凡的性能。作为天然蛋白质生物材料平台,蚕丝纳米纤维已加工成膜,海绵,凝胶和支架等形式的各种材料。
刺激响应高分子材料能对外界刺激产生快速响应,在生物传感、检测、载药等领域具有很好的应用前景。响应型高分子体系可以用于各种应用,例如可控表面和粘合剂,适应环境的防护涂层,人造肌肉,传感器以及载药。生物化学,环境科学和生物医学仅仅是重要应用领域的几个例子,刺激响应型高分子材料还有更大的发展空间。响应型的粒子具有复杂的、分层的结构以适应各种可能的机制。分层结构同样对接受信号和通过改变材料性质的来响应的功能进行分离的体系的发展很重要。因为,在某些情况下,刺激所引起的变化可能干扰材料性质所预期的变化。刺激响应型材料中这样的组织将为材料的可设计性以及复杂响应提供更大的机会,另一个挑战是开发以一种智能的方式可以对多种刺激响应的体系,长期稳定性和耐久性仍是这种体系的重大挑战。刺激响应型体系可以相对低成本地引入更多产品,因为通常只需要很薄的涂层(纳米厚度,通过增加这样功能性的涂层可以显著地提高产品的价值。
生物蛋白质纤维蜘蛛丝具有优异的力学性能、精巧的分级结构和潜在的应用前景。研究显示这种大壶状腺丝对水敏感,具有“超收缩”性能,当相对湿度达到一定水平时,其可在长度方向上收缩约50%。蜘蛛丝的超收缩性能使其在人造肌肉或拉伸驱动器领域具有潜在的应用价值。当相对湿度达到约70%时,蜘蛛大壶状腺丝开始产生超过每毫米300度的扭转变形。同样作为动物蛋白纤维,这一明显的湿敏响应性在在蚕丝蛋白纤维中尚未被发现。部分原因可能因为蜘蛛丝的尺寸比蚕丝小,比表面大,表面基团更丰富。目前,剥离纳米纤维获得更小尺寸的方法主要有机械法、静电纺、熔喷等方法,静电纺以及熔喷法需要将天然蚕丝先溶解,溶解过程将天然蚕丝的结晶完全破坏,而机械剥离法单纯将蚕丝的尺寸变得更小,而对剥离后蚕丝的表面结构影响不大。本申请使用低共熔深度溶剂将蚕丝蛋白纤维剥离,剥离后可以得到不同尺寸的纤丝,多层次尺寸的纤丝具有不同的结构,一方面较好的保持了天然蚕丝优良的力学性能,另外一方面经过深度溶剂中氯化胆碱的处理纤丝表面具备丰富的基团,其中亲水性较好的silkI结晶可以与环境中的水分以及部分气体产生具有丰富的作用,并受温度的影响。通过自组装构成的膜材料由于具有致密的结构,当控制材料两侧温度差、湿度差或者环境中气体浓度差,纤丝膜材料可以发生快速发生弯曲、折叠以及支撑重物的行为,在形状记忆、环境监测以及人工机器人等领域具有广泛的应用前景。
发明内容
本发明提出一种蚕丝蛋白环境刺激响应致动器件的制备方法及使用方法,在形状记忆、环境监测以及人工机器人领域具有广泛应用前景。
为实现上述目的,本发明采用的技术方案为:
(1)将丝素蛋白纤维分散在低共熔深度溶剂中,然后通过升温、搅拌处理将丝素蛋白纤维剥离成纤丝。其中蚕丝蛋白纤维的来源包括榨蚕丝和桑蚕丝,优选桑蚕丝;
(2)将步骤(1)制备得到的低共熔深度溶剂-纤丝分散体系装入透析袋中在水中透析,为控制纤丝分散液的浓度,然后再将透析液放到聚乙烯醇中进行浓缩。
(3)将步骤(2)中的纤丝浓缩液进行蒸发自组装,最后得到致动器件。
本发明技术方案中,所述低共熔深度溶剂包括尿素-氯化胆碱和硫脲-氯化胆碱体系,其中尿素或者硫脲与氯化胆碱的摩尔比为5:1-10:1;蚕丝蛋白纤维与低共熔深度溶剂的质量比为1:20-1:40;低共熔深度溶剂处理蚕丝蛋白纤维的温度为80-100℃,处理时间为3h-24h。
本发明技术方案中,透析低共熔深度溶剂的透析袋截留分子量为10000-14000,浓缩纤丝透析液所用的聚乙烯醇的分子量为8000-10000,浓缩后纤丝的浓度为1 wt%-3 wt%。
本发明技术方案中,纤丝浓缩液进行自组装时浓缩液液膜的厚度为5mm-8mm,纤丝浓缩液进行自组装时控制环境湿度为40%-70%。最终得到的致动器中直径为30nm-100nm的纤丝的质量百分数为50%-70%,直径为100nm-500nm纤丝的质量百分数为20%-40%,直径为1μm-5μm纤丝的质量百分数为10%-30%。
本发明技术方案中,一种蚕丝蛋白环境刺激响应致动器件的使用方法,在制备好的蚕丝纤丝自组装器件两侧控制不同的湿度差、温度差或者气体浓度差实现自动弯曲、折叠、支撑等运动行为。其中湿度差控制在30%-70%之间;温度差控制在20℃-50℃之间;可使用的气体应具备可形成氢键的官能团,优选乙醇和氨气。
本发明的技术原理
本发明采用尿素-氯化胆碱或硫脲-氯化胆碱体系,破坏非共价键(如氢键)并降低蛋白质中疏水相互作用的强度,进而将蚕丝纤维直接剥落成纤丝。蚕丝纤维被剥离为纤丝的过程中非晶区被破坏,晶区受影响较小。然而silkI的衍射峰明显增强,即在结晶区所占比例升高,silkI具有较好的亲水性;此外蚕丝被剥离为纤丝过程中,比表面增大,有更多的氨基酸残基暴露。
利用蒸发自组装的方法得到纤丝膜,纤丝膜由不同尺寸的纤丝构成,不同尺寸的纤丝具有不同的结构,其中尺寸比较大的纤丝较好的保留了非晶区,使膜材料具有较好的韧性,尺寸比较小的纤丝结晶区比例较高,具有较好的刚性。
组成蚕丝的氨基酸具有丰富的基团,蚕丝被剥离为纤丝后,比表面变大,有更多的氨基酸残基暴露出来,此外,由纤丝自组装构成的膜具有一定的阻隔性能,当膜两边的环境不一样时,膜的结构会发生变化,例如当膜一侧湿度增加时,该侧纤丝会吸水发生溶胀,进而会发生弯曲等致动行为,当两边环境恢复一样时,膜重新恢复原样。
本发明的优势
1.本发明使用低共熔深度溶剂制备纤丝,过程绿色,简单高效,仅仅依靠破坏蚕丝的非共价键将蚕丝剥离,较好的保护了蚕丝的独特的结晶结构、生物相容性和安全性。
2.剥离得到的纤丝具有较高的比表面,表面具有大量的氨基酸残基,且纤丝具有不同的多级结构,此外,纤丝膜较好的阻滤性能。当膜两边的环境不同时,上述特点共同导致纤丝材料具有环境响应性,包括湿度、温度以及气体。且纤维的多级结构导致自组装的纤丝膜具有优良的耐疲劳性能,使用1000个周期后仍然保持较好的效果。
附图说明
图1是蚕丝蛋白纳米纤维电镜示意图。
图2是蚕丝(silk ⅡⅠ)及经过处理制得的纤丝的X-射线衍射谱图。
图3 a、图3b分别是纤丝致动器膜在湿度差为0%和湿度差为30%(手指有湿气)的弯曲图。
具体实施方式
下面结合附图和具体实施例,对本发明技术方案作进一步阐述。
实施例1
将桑蚕丝丝素蛋白纤维分散在尿素-氯化胆碱低共熔深度溶剂中,其中尿素与氯化胆碱的摩尔比为5:1,蚕丝蛋白纤维与低共熔深度溶剂的质量比为1:20;然后通过升温、搅拌处理将丝素蛋白纤维剥离成纤丝,低共熔深度溶剂处理蚕丝蛋白纤维的温度为80℃,处理时间为3h;将制得的低共熔深度溶剂-纤丝分散体系装入透析袋中并在蒸馏水中透析,然后再将透析液放到聚乙烯醇中进行浓缩,透析低共熔深度溶剂的透析袋截留分子量为10000,浓缩纤丝透析液所用的聚乙烯醇的分子量为8000,浓缩后纤丝的浓度为1wt%;将步骤(2)中的纤丝浓缩液进行蒸发自组装,纤丝浓缩液进行自组装时浓缩液液膜的厚度为5mm,环境湿度为40%;最后得到致动器件,致动器中直径为30nm-100nm的纤丝的质量百分数为50%,直径为100nm-500nm的纤丝的质量百分数为30%,直径为1μm-5μm的纤丝的质量百分数为20%。
控制制备好的纤丝致动器膜两侧湿度差为30%,1.1s时膜弯曲的角度达到50°;将两边的湿度差恢复为完全一样时,致动器膜恢复为平展状态;重复该循环1000次后,膜弯曲的角度达到48°,致动器膜两侧湿度一样时仍可以恢复到平展状态。
实施例2
将桑蚕丝丝素蛋白纤维分散在尿素-氯化胆碱低共熔深度溶剂中,其中尿素与氯化胆碱的摩尔比为10:1,蚕丝蛋白纤维与低共熔深度溶剂的质量比为1:40;然后通过升温、搅拌处理将丝素蛋白纤维剥离成纤丝,低共熔深度溶剂处理蚕丝蛋白纤维的温度为100℃,处理时间为24h;将制得的低共熔深度溶剂-纤丝分散体系装入透析袋中并在蒸馏水中透析,然后再将透析液放到聚乙烯醇中进行浓缩,透析低共熔深度溶剂的透析袋截留分子量为14000,浓缩纤丝透析液所用的聚乙烯醇的分子量为10000,浓缩后纤丝的浓度为2wt%;将步骤(2)中的纤丝浓缩液进行蒸发自组装,纤丝浓缩液进行自组装时浓缩液液膜的厚度为8mm,环境湿度为50%;最后得到致动器件,致动器中直径为30nm-100nm的纤丝的质量百分数为70%,直径为100nm-500nm的纤丝的质量百分数为25%,直径为1μm-5μm的纤丝的质量百分数为5%。
控制制备好的纤丝致动器膜两侧湿度差为70%,0.7s时膜弯曲的角度达到150°;将两边的湿度差恢复为完全一样时,致动器膜恢复为平展状态;重复该循环1000次后,膜弯曲的角度达到139°,致动器膜两侧湿度一样时仍可以恢复到平展状态。
实施例3
将柞蚕丝素蛋白纤维分散在硫脲-氯化胆碱低共熔深度溶剂中,其中硫脲与氯化胆碱的摩尔比为8:1,蚕丝蛋白纤维与低共熔深度溶剂的质量比为1:30;然后通过升温、搅拌处理将丝素蛋白纤维剥离成纤丝,低共熔深度溶剂处理蚕丝蛋白纤维的温度为90℃,处理时间为6h;将制得的低共熔深度溶剂-纤丝分散体系装入透析袋中并在蒸馏水中透析,然后再将透析液放到聚乙烯醇中进行浓缩,透析低共熔深度溶剂的透析袋截留分子量为14000,浓缩纤丝透析液所用的聚乙烯醇的分子量为10000,浓缩后纤丝的浓度为1.5wt%;将步骤(2)中的纤丝浓缩液进行蒸发自组装,纤丝浓缩液进行自组装时浓缩液液膜的厚度为6mm,环境湿度为60%;最后得到致动器件,致动器中直径为30nm-100nm的纤丝的质量百分数为70%,直径为100nm-500nm的纤丝的质量百分数为27%,直径为1μm-5μm的纤丝的质量百分数为3%。
当环境湿度为50%,控制制备好的纤丝致动器膜两侧温度差为4°C,3.4s时膜弯曲的角度达到40°;将两边的温度差恢复为完全一样时,致动器膜恢复为平展状态;重复该循环500次后,膜弯曲的角度达到36°,致动器膜两侧温度一样时仍可以恢复到平展状态。
实施例4
将柞蚕丝素蛋白纤维分散在尿素-氯化胆碱低共熔深度溶剂中,其中尿素与氯化胆碱的摩尔比为6:1,蚕丝蛋白纤维与低共熔深度溶剂的质量比为1:30;然后通过升温、搅拌处理将丝素蛋白纤维剥离成纤丝,低共熔深度溶剂处理蚕丝蛋白纤维的温度为80℃,处理时间为15h;将制得的低共熔深度溶剂-纤丝分散体系装入透析袋中并在蒸馏水中透析,然后再将透析液放到聚乙烯醇中进行浓缩,透析低共熔深度溶剂的透析袋截留分子量为12000,浓缩纤丝透析液所用的聚乙烯醇的分子量为9000,浓缩后纤丝的浓度为1.8wt%;将步骤(2)中的纤丝浓缩液进行蒸发自组装,纤丝浓缩液进行自组装时浓缩液液膜的厚度为6mm,环境湿度为50%;最后得到致动器件,致动器中直径为30nm-100nm的纤丝的质量百分数为55%,直径为100nm-500nm的纤丝的质量百分数为25%,直径为1μm-5μm的纤丝的质量百分数为20%。
当环境湿度为50%,温度为30°C,控制制备好的纤丝致动器膜两侧氨气的浓度差为0.1mol/L,5.6s时膜弯曲的角度达到50.5°;将两边的氨气浓度恢复为完全一样时,致动器膜恢复为平展状态;重复该循环200次后,膜弯曲的角度达到45°,致动器膜两侧氨气浓度一样时仍可以恢复到平展状态。
当环境湿度为50%,温度为30°C,控制制备好的纤丝致动器膜两侧乙醇的浓度差为0.1mol/L,5.2s时膜弯曲的角度达到70.3°;将两边的乙醇浓度恢复为完全一样时,致动器膜恢复为平展状态;重复该循环200次后,膜弯曲的角度达到67°,致动器膜两侧乙醇浓度一样时仍可以恢复到平展状态。
Claims (3)
1.一种蚕丝丝素蛋白环境刺激响应致动器件的制备方法,包括剥离、透析洗涤和自组装三步,具体步骤如下:
(1)将蚕丝丝素蛋白纤维分散在低共熔深度溶剂中,然后通过升温、搅拌处理将蚕丝丝素蛋白纤维剥离成纤丝,其中蚕丝丝素蛋白纤维选自榨蚕丝或桑蚕丝;
(2)将步骤(1)制备得到的低共熔深度溶剂-纤丝分散体系装入透析袋中并在蒸馏水中透析,然后再将透析液放到聚乙烯醇中进行浓缩;
(3)将步骤(2)中的纤丝浓缩液进行蒸发自组装,最后得到致动器件;
透析低共熔深度溶剂的透析袋截留分子量为10000-14000,浓缩纤丝透析液所用的聚乙烯醇的分子量为8000-10000,浓缩后纤丝的浓度为1 wt%-3 wt%;
步骤(1)中所述低共熔深度溶剂选自尿素-氯化胆碱或硫脲-氯化胆碱体系,其中尿素或者硫脲与氯化胆碱的摩尔比为5:1-10:1;蚕丝丝素蛋白纤维与低共熔深度溶剂的质量比为1:20-1:40;低共熔深度溶剂处理蚕丝丝素蛋白纤维的温度为80℃-100℃,处理时间为3h-24h。
2.按权利要求1所述的蚕丝丝素蛋白环境刺激响应致动器件的制备方法,其特征在于:纤丝浓缩液进行自组装时浓缩液液膜的厚度为5mm-8mm,纤丝浓缩液进行自组装时控制环境湿度为40-70%;最终制得的致动器中直径为30nm-100nm的纤丝的质量百分数为50%-70%,直径为100nm-500nm的纤丝的质量百分数为20%-40%,直径为1μm-5μm的纤丝的质量百分数为10%-30%。
3.一种如权利要求1或2之一所述的制备方法制备的蚕丝丝素蛋白环境刺激响应致动器件的使用方法,在制备好的蚕丝丝素蛋白环境刺激响应致动器件两侧控制不同的湿度差、温度差或者气体浓度差实现自动弯曲、折叠、支撑这些运动行为;其中湿度差控制在30%-70%之间;温度差控制在20℃-50℃之间;使用的气体选自氨气。
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CN102743796A (zh) * | 2011-04-18 | 2012-10-24 | 北京汇亨创管理咨询有限公司 | 用聚乙烯醇制成的丝素蛋白多孔支架及其制备方法和用途 |
CN108022761A (zh) * | 2017-12-28 | 2018-05-11 | 中国人民大学 | 一种蚕丝纳米纤维膜及其制备方法与在超级电容器中的应用 |
CN108467427A (zh) * | 2018-03-27 | 2018-08-31 | 南通纺织丝绸产业技术研究院 | 利用低共熔溶剂溶解羊毛制备角蛋白的方法 |
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Patent Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN102743796A (zh) * | 2011-04-18 | 2012-10-24 | 北京汇亨创管理咨询有限公司 | 用聚乙烯醇制成的丝素蛋白多孔支架及其制备方法和用途 |
CN108022761A (zh) * | 2017-12-28 | 2018-05-11 | 中国人民大学 | 一种蚕丝纳米纤维膜及其制备方法与在超级电容器中的应用 |
CN108467427A (zh) * | 2018-03-27 | 2018-08-31 | 南通纺织丝绸产业技术研究院 | 利用低共熔溶剂溶解羊毛制备角蛋白的方法 |
Non-Patent Citations (2)
Title |
---|
"Controllable exfoliation of natural silk fibers into nanofibrils by protein denaturant deep eutectic solvent:nanofibrous strategy for multifunctional membranes";Xingxing Tan 等;《Green Chemistry》;20180702;第20卷;第3625-3633页 * |
"南开大学团队研获纯蚕丝"人工肌肉"可用于智能织物及柔性机器人";中国纺织网;《化纤与纺织技术》;20190315;第48卷(第1期);第38页 * |
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