覆盖率和客体残基对聚脯氨酸II螺旋肽抗污性能的影响。
Impact of coverage and guest residue on polyproline II helix peptide antifouling.
作者信息
Ahn Rebecca S, Grome Henry T, Asaei Sogol, Verma Geeta, Dang Christina S, Baskaran Harihara, Renner Julie N
机构信息
Department of Chemical and Biomolecular Engineering, Case Western Reserve University, Cleveland, USA.
出版信息
MRS Commun. 2024;14(6):1134-1141. doi: 10.1557/s43579-024-00674-w. Epub 2024 Nov 11.
UNLABELLED
Polyproline II (PPII) peptide sequences are recognized as promising biomaterials because of their attractive antifouling properties. However, the mechanisms behind their antifouling behavior have not been fully characterized. In this work we show that PPII peptide coverage, controlled by adsorption time, significantly reduces the fouling of bovine serum albumin (BSA, a model foulant). In addition, guest residues introduced into the PPII sequence are shown to significantly impact BSA adsorption as well as human mesenchymal stem cell (hMSC) spreading. This research will help guide future PPII peptide designs for incorporation into novel biomaterials.
GRAPHICAL ABSTRACT
A guest residue system was utilized to understand properties that impact the ability of polyproline II helix peptide monolayers to resist the fouling of BSA and influence human mesenchymal cell spreading.
SUPPLEMENTARY INFORMATION
The online version contains supplementary material available at 10.1557/s43579-024-00674-w.
未标记
聚脯氨酸II（PPII）肽序列因其具有吸引人的抗污性能而被认为是有前景的生物材料。然而，其抗污行为背后的机制尚未完全阐明。在这项工作中，我们表明通过吸附时间控制的PPII肽覆盖率显著降低了牛血清白蛋白（BSA，一种模型污垢物）的污染。此外，引入到PPII序列中的客体残基被证明会显著影响BSA的吸附以及人间充质干细胞（hMSC）的铺展。这项研究将有助于指导未来用于新型生物材料的PPII肽设计。
图形摘要
利用客体残基系统来了解影响聚脯氨酸II螺旋肽单层抵抗BSA污染和影响人间充质细胞铺展能力的特性。
补充信息
在线版本包含可在10.1557/s43579-024-00674-w获取的补充材料。
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