Mechanical properties of the P-selectin/PSGL-1 interaction

Author

Marshall, B.T. ; McEver, R.P. ; Zhu, C.

Author_Institution

Sch. of Mech. Eng., Georgia Inst. of Technol., Atlanta, GA, USA

Volume

1

fYear

2002

fDate

2002

Firstpage

337

Abstract

Using an Atomic Force Microscope (AFM), the mechanical properties of the P-selectin/PSGL-1 complex were studied with two separate methods. Both methods yielded similar results. The molecular complex displayed a linear relationship between force and molecular extension. The dimeric bond of the wild type PSGL-1 interaction resulted in a spring constant roughly double that of a recombinant monomeric PSGL-1 interaction, suggesting that the two subunits of the dimeric interaction act as springs in parallel. The P-selectin portion of the complex was found to contribute the most to the mechanical compliance of the molecular complex.

Keywords

atomic force microscopy; biomechanics; haemorheology; molecular biophysics; proteins; AFM; P-selectin/PSGL-1 interaction; dimeric bond; dimeric interaction; mechanical compliance; mechanical properties; molecular complex; molecular extension; spring constant; Adhesives; Atomic force microscopy; Atomic measurements; Bonding; Fluctuations; Force measurement; Mechanical factors; Polymers; Springs; White blood cells;

fLanguage

English

Publisher

ieee

Conference_Titel

Engineering in Medicine and Biology, 2002. 24th Annual Conference and the Annual Fall Meeting of the Biomedical Engineering Society EMBS/BMES Conference, 2002. Proceedings of the Second Joint

ISSN

1094-687X

Print_ISBN

0-7803-7612-9

Type

conf

DOI

10.1109/IEMBS.2002.1134523

Filename

1134523