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Filtering by: DOI 10.1116/1.4767124 Creator Baio, Joe E.

Full membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptides

Creator:

Franz, Johannes, Graham, Daniel J., Schmüser, Lars, Baio, Joe E., Lelle, Marco, Peneva, Kalina, Müllen, Klaus, Castner, David G., Bonn, Mischa, and Weidnera, Tobias

Abstract:

Biophysical studies of the interaction of peptides with model membranes provide a simple yet effective approach to understand the transport of peptides and peptide based drug carriers across the cell membrane. Herein, the authors discuss the use of self-assembled monolayers fabricated from the full membrane-spanning thiol (FMST) 3-((14-((40-((5-methyl-1-phenyl-35-(phytanyl)oxy- 6,9,12,15,18,21,24,27,30,33,37-undecaoxa-2,3-dithiahenpentacontan-51-yl)oxy)-[1,10-biphenyl]-4- yl)oxy)tetradecyl)oxy)-2-(phytanyl)oxy...

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Article

Full Text:

, 10(1), 019009. doi:10.1116/1.4908164 10.1116/1.4908164 American Institute of Physics Publishing
Differential surface activation of the A1 domain of von Willebrand factor

Creator:

Tronic, Elaine H., Yakovenko, Olga, Weidner, Tobias, Baio, Joe E., Penkala, Rebecca, Castner, David G., and Thomas, Wendy E.

Abstract:

The clotting protein von Willebrand factor (VWF) binds to platelet receptor glycoprotein Ibα (GPIbα) when VWF is activated by chemicals, high shear stress, or immobilization onto surfaces. Activation of VWF by surface immobilization is an important problem in the failure of cardiovascular implants, but is poorly understood. Here, the authors...

Resource Type:

Article

Full Text:

(http://creativecommons.org/licenses/by /4.0/). [http://dx.doi.org/10.1116/1.4943618] I. INTRODUCTION

ScholarsArchive@OSU

Full membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptides

Differential surface activation of the A1 domain of von Willebrand factor

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