Development of a novel papain gel formulation: Exploring different concentrations for smear-layer deproteinization and enhanced dentin bonding.

IF 3.6 3区 综合性期刊 Q1 MULTIDISCIPLINARY SCIENCES Heliyon Pub Date : 2024-10-05 eCollection Date: 2024-10-15 DOI:10.1016/j.heliyon.2024.e39035
Citra Kusumasari, Ratna Meidyawati, Aryo Megantoro, Rachendra Tiara, Agita Meiskya, Khaled M Darwish, Ahmed Abdou
{"title":"Development of a novel papain gel formulation: Exploring different concentrations for smear-layer deproteinization and enhanced dentin bonding.","authors":"Citra Kusumasari, Ratna Meidyawati, Aryo Megantoro, Rachendra Tiara, Agita Meiskya, Khaled M Darwish, Ahmed Abdou","doi":"10.1016/j.heliyon.2024.e39035","DOIUrl":null,"url":null,"abstract":"<p><strong>Background: </strong>The self-etch adhesive system modifies but does not completely remove the smear layer, leading to the weakening of the bond strength due to the formation of a hybridized layer. Smear-layer deproteinization with papain enzyme partially removes the smear layer, and increases the bond strength with self-etch adhesive. The aim was to develop a deproteinizing agent with a high papain enzyme concentration to enhance dentin bonding with self-etch adhesives.</p><p><strong>Methods: </strong>Papain enzyme gel formulations (15 and 30 IU/g) were prepared and tested for physical stability, viscosity, pH, homogeneity, and organoleptic properties. Moreover, 64 teeth were used to test the deproteinization efficiency of the formed gel. Fourier transform infrared was used to calculate the ratio of organic to inorganic components of smear-layer after deproteinization with 15 and 30 IU/g papain gel and a 6 IU/g commercial papain gel. Moreover, tensile bond strength was measured after deproteinization and dentin bonding with self-etching adhesive for the same groups. A molecular modeling simulation was also performed to evaluate the protein-protein binding interaction, predict the conformational/orientation patterns, and estimate the binding energies of papain with collagen target protein.</p><p><strong>Results: </strong>Both 15 and 30 IU/g gels exhibited similar viscosity, pH, homogeneity, and organoleptic properties. However, after 60 s, the 15 IU/g gel was solid, while the 30 IU/g gel was half-solid. All tested groups decreased the amide:phosphate ratio and increased tensile bond strength. Binding complexes between papain and three deposited collagen-1 structures formed strong binding energies with high negative values and residue-wise binding patterns.</p><p><strong>Conclusions: </strong>The production of the papain enzyme gel with a concentration of 15 IU/g was successful. In addition, it demonstrated promising results when used as a smear-layer deproteinization agent.</p><p><strong>Clinical significance: </strong>Enzymatic smear-layer deproteinization may improve dentin adhesion, and high concertation papain enzyme gels may improve dentin adhesion with the use of self-etch adhesive.</p>","PeriodicalId":12894,"journal":{"name":"Heliyon","volume":"10 19","pages":"e39035"},"PeriodicalIF":3.6000,"publicationDate":"2024-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11492583/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Heliyon","FirstCategoryId":"103","ListUrlMain":"https://doi.org/10.1016/j.heliyon.2024.e39035","RegionNum":3,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/10/15 0:00:00","PubModel":"eCollection","JCR":"Q1","JCRName":"MULTIDISCIPLINARY SCIENCES","Score":null,"Total":0}
引用次数: 0

Abstract

Background: The self-etch adhesive system modifies but does not completely remove the smear layer, leading to the weakening of the bond strength due to the formation of a hybridized layer. Smear-layer deproteinization with papain enzyme partially removes the smear layer, and increases the bond strength with self-etch adhesive. The aim was to develop a deproteinizing agent with a high papain enzyme concentration to enhance dentin bonding with self-etch adhesives.

Methods: Papain enzyme gel formulations (15 and 30 IU/g) were prepared and tested for physical stability, viscosity, pH, homogeneity, and organoleptic properties. Moreover, 64 teeth were used to test the deproteinization efficiency of the formed gel. Fourier transform infrared was used to calculate the ratio of organic to inorganic components of smear-layer after deproteinization with 15 and 30 IU/g papain gel and a 6 IU/g commercial papain gel. Moreover, tensile bond strength was measured after deproteinization and dentin bonding with self-etching adhesive for the same groups. A molecular modeling simulation was also performed to evaluate the protein-protein binding interaction, predict the conformational/orientation patterns, and estimate the binding energies of papain with collagen target protein.

Results: Both 15 and 30 IU/g gels exhibited similar viscosity, pH, homogeneity, and organoleptic properties. However, after 60 s, the 15 IU/g gel was solid, while the 30 IU/g gel was half-solid. All tested groups decreased the amide:phosphate ratio and increased tensile bond strength. Binding complexes between papain and three deposited collagen-1 structures formed strong binding energies with high negative values and residue-wise binding patterns.

Conclusions: The production of the papain enzyme gel with a concentration of 15 IU/g was successful. In addition, it demonstrated promising results when used as a smear-layer deproteinization agent.

Clinical significance: Enzymatic smear-layer deproteinization may improve dentin adhesion, and high concertation papain enzyme gels may improve dentin adhesion with the use of self-etch adhesive.

Abstract Image

Abstract Image

Abstract Image

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
开发新型木瓜蛋白酶凝胶配方:探索不同浓度的涂片层脱蛋白和增强牙本质粘接效果。
背景:自酸蚀粘合剂系统能改变但不能完全去除涂抹层,从而形成杂化层,导致粘合强度减弱。用木瓜蛋白酶对涂抹层进行去蛋白处理可部分去除涂抹层,并提高自酸蚀粘合剂的粘合强度。目的是开发一种高浓度木瓜蛋白酶去蛋白剂,以增强自酸蚀粘合剂的牙本质粘合力:方法:制备木瓜蛋白酶凝胶配方(15 和 30 IU/g),并测试其物理稳定性、粘度、pH 值、均匀性和感官特性。此外,还用 64 颗牙齿测试了所制凝胶的去蛋白效率。使用 15 和 30 IU/g 的木瓜蛋白酶凝胶以及 6 IU/g 的商用木瓜蛋白酶凝胶进行去蛋白后,用傅立叶变换红外线计算涂片层中有机成分和无机成分的比例。此外,还测量了同组牙本质脱蛋白和使用自酸蚀粘合剂粘接牙本质后的拉伸粘接强度。此外,还进行了分子建模模拟,以评估蛋白质与蛋白质之间的结合相互作用,预测木瓜蛋白酶的构象/定向模式,并估算木瓜蛋白酶与胶原目标蛋白的结合能:结果:15 和 30 IU/g 的凝胶具有相似的粘度、pH 值、均匀性和感官特性。然而,60 秒后,15 IU/g 凝胶为固体,而 30 IU/g 凝胶为半固体。所有测试组都降低了酰胺与磷酸盐的比率,提高了拉伸粘接强度。木瓜蛋白酶与三种沉积的胶原蛋白-1结构之间的结合复合物形成了高负值的强结合能和残基结合模式:结论:浓度为 15 IU/g 的木瓜蛋白酶凝胶的生产是成功的。结论:浓度为 15 IU/g 的木瓜蛋白酶凝胶的生产是成功的,此外,它在用作涂片层脱蛋白剂时也表现出了良好的效果:临床意义:酶涂片层脱蛋白可改善牙本质粘附性,高协同木瓜蛋白酶凝胶可改善使用自酸蚀粘合剂时的牙本质粘附性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
Heliyon
Heliyon MULTIDISCIPLINARY SCIENCES-
CiteScore
4.50
自引率
2.50%
发文量
2793
期刊介绍: Heliyon is an all-science, open access journal that is part of the Cell Press family. Any paper reporting scientifically accurate and valuable research, which adheres to accepted ethical and scientific publishing standards, will be considered for publication. Our growing team of dedicated section editors, along with our in-house team, handle your paper and manage the publication process end-to-end, giving your research the editorial support it deserves.
期刊最新文献
Corrigendum to "Short-term outcomes of robot-assisted minimally invasive surgery for brainstem hemorrhage: A case-control study" [Heliyon Volume 10, Issue 4, February 2024, Article e25912]. Retraction notice to "Enhancing data security and privacy in energy applications: Integrating IoT and blockchain technologies" [Heliyon 10 (2024) e38917]. Retraction notice to "CREB1 promotes cholangiocarcinoma metastasis through transcriptional regulation of the LAYN-mediated TLN1/β1 integrin axis" [Heliyon 10 (2024) e36595]. Retraction notice to "Experimental investigations of dual functional substrate integrated waveguide antenna with enhanced directivity for 5G mobile communications" [Heliyon 10 (2024) e36929]. Retraction notice to "Nutritional and bioactive properties and antioxidant potential of Amaranthus tricolor, A. lividus, A viridis, and A. spinosus leafy vegetables" [Heliyon 10 (2024) e30453].
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1