Biophysical characterization of blood coagulation factor VIII binding to lipid nanodiscs that mimic activated platelet surfaces.

ABSTRACT:

Background

Following proteolytic activation, activated blood coagulation factor (F)VIII (FVIIIa) binds to activated platelet membranes, forming the intrinsic tenase complex with activated FIX (FIXa). Previous studies have identified the C1 and C2 domains as the membrane binding domains of FVIII through conserved arginine residues. A membrane binding model for the FVIII C domains proposes that surface-exposed hydrophobic and positively charged residues at each C domain interact with the membrane, yet a comprehensive thermodynamic and structural description of this interaction is lacking.

Objectives

To determine residues of interaction, thermodynamics, and membrane binding preference for FVIII membrane association.

Methods

The binding of FVIII constructs to lipid nanodi

SUBMITTER: Avery NG 

PROVIDER: S-EPMC11786986 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature