Our official English website, www.x-mol.net, welcomes your
feedback! (Note: you will need to create a separate account there.)
Platelet Adhesion and Activation on Chiral Surfaces: The Influence of Protein Adsorption
Langmuir ( IF 3.7 ) Pub Date : 2017-09-20 00:00:00 , DOI: 10.1021/acs.langmuir.7b02283 Yonghong Fan 1, 2 , Rifang Luo 3 , Honghong Han 1, 2 , Yajun Weng 1, 2 , Hong Wang 1, 2 , Jing’an Li 1, 2 , Ping Yang 1, 2 , Yunbing Wang 3 , Nan Huang 1, 2
Langmuir ( IF 3.7 ) Pub Date : 2017-09-20 00:00:00 , DOI: 10.1021/acs.langmuir.7b02283 Yonghong Fan 1, 2 , Rifang Luo 3 , Honghong Han 1, 2 , Yajun Weng 1, 2 , Hong Wang 1, 2 , Jing’an Li 1, 2 , Ping Yang 1, 2 , Yunbing Wang 3 , Nan Huang 1, 2
Affiliation
|
Adsorbed proteins and their conformational change on blood-contacting biomaterials will determine their final hemocompatibility. It has frequently been reported that surface chirality of biomaterials may highly influence their protein adsorption behavior. Here, lysine and tartaric acid with different chirality were immobilized onto TiO2 films respectively, and the influence of surface chirality on protein adsorption, platelet adhesion, and activation was also investigated. It showed that the l- and d-molecule grafted samples had almost the same grafting density, surface topography, chemical components, and hydrophilicity in this study. However, biological behaviors such as protein adsorption, platelet adhesion, and activation were quite different. The d-lysine grafted surface had a greater ability to inhibit both bovine serum albumin and fibrinogen adsorption, along with less degeneration of fibrinogen compared to the l-lysine anchored surface. However, the d-tartaric acid grafted surface adsorbed more protein but with less denatured fibrinogen compared to the l-tartaric acid grafted one. Further studies showed that the secondary structural change of the adsorbed albumin and fibrinogen on all surfaces with deduction of the α-helix content and increase of disordered structure, while the changing degree was apparently varied. As a result, the d-lysine immobilized surface absorbed less platelets and red blood cells and achieved slightly increased platelet activation. For tartaric acid anchored surfaces, a larger number of platelets adhered to the D-surface but were less activated compared to the L-surface. In conclusion, the surface chirality significantly influenced the adsorption and conformational change of blood plasma protein, which in turn influenced both platelet adhesion and activation.
中文翻译：
血小板在手性表面上的粘附和活化：蛋白质吸附的影响
血液接触生物材料上吸附的蛋白质及其构象变化将决定其最终的血液相容性。经常有报道说，生物材料的表面手性可能会严重影响其蛋白质的吸附行为。在此，将手性不同的赖氨酸和酒石酸分别固定在TiO 2膜上，并研究了表面手性对蛋白质吸附，血小板粘附和活化的影响。结果表明，在本研究中，L和D分子接枝的样品具有几乎相同的接枝密度，表面形貌，化学成分和亲水性。但是，诸如蛋白质吸附，血小板粘附和活化的生物学行为是完全不同的。这与l-赖氨酸锚定的表面相比，d-赖氨酸移植的表面具有更大的抑制牛血清白蛋白和纤维蛋白原吸附的能力，以及更少的纤维蛋白原变性。然而，与1-酒石酸接枝的表面相比，d-酒石酸接枝的表面吸附了更多的蛋白质，但变性纤维蛋白原较少。进一步的研究表明，吸附的白蛋白和纤维蛋白原在所有表面上的二级结构变化都伴随着α-螺旋含量的减少和无序结构的增加，而变化程度却明显不同。结果，d赖氨酸固定化的表面吸收较少的血小板和红细胞，并实现了略微增加的血小板活化。对于酒石酸锚定的表面，与L表面相比，有更多的血小板粘附于D表面，但活化程度较低。总之，表面手性显着影响血浆蛋白的吸附和构象变化，进而影响血小板粘附和激活。
更新日期：2017-09-20
中文翻译：
血小板在手性表面上的粘附和活化：蛋白质吸附的影响
血液接触生物材料上吸附的蛋白质及其构象变化将决定其最终的血液相容性。经常有报道说，生物材料的表面手性可能会严重影响其蛋白质的吸附行为。在此，将手性不同的赖氨酸和酒石酸分别固定在TiO 2膜上，并研究了表面手性对蛋白质吸附，血小板粘附和活化的影响。结果表明，在本研究中，L和D分子接枝的样品具有几乎相同的接枝密度，表面形貌，化学成分和亲水性。但是，诸如蛋白质吸附，血小板粘附和活化的生物学行为是完全不同的。这与l-赖氨酸锚定的表面相比，d-赖氨酸移植的表面具有更大的抑制牛血清白蛋白和纤维蛋白原吸附的能力，以及更少的纤维蛋白原变性。然而，与1-酒石酸接枝的表面相比，d-酒石酸接枝的表面吸附了更多的蛋白质，但变性纤维蛋白原较少。进一步的研究表明，吸附的白蛋白和纤维蛋白原在所有表面上的二级结构变化都伴随着α-螺旋含量的减少和无序结构的增加，而变化程度却明显不同。结果，d赖氨酸固定化的表面吸收较少的血小板和红细胞，并实现了略微增加的血小板活化。对于酒石酸锚定的表面，与L表面相比，有更多的血小板粘附于D表面，但活化程度较低。总之，表面手性显着影响血浆蛋白的吸附和构象变化，进而影响血小板粘附和激活。
京公网安备 11010802027423号