June 1, 2011Journal of Biological ChemistryOpen Access

Increasing Hydrophobicity or Disulfide Bridging at the Factor VIII A1 and C2 Domain Interface Enhances Procofactor Stability

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Population

Factor VIII (FVIII) protein variants

Comparison

Generation of FVIII variants with a disulfide… vs Wild-type (WT) FVIII

Design

Preclinical

Authors

HWHironao WakabayashiUniversity of Rochester Medical Center AGAmy E. GriffithsPennsylvania State University PFPhilip J. FayPhilips (Finland)

Discussion

Member takes

Implication

These FVIII variants remain preclinical; leaves open potential for engineered hemophilia therapies pending further validation.

Structured PICO

Population

Factor VIII (FVIII) protein variants

Intervention

Generation of FVIII variants with a disulfide bond between A1 and C2 domains (R121C/L2302C) or increased hydrophobicity (A108I)

Comparator

Wild-type (WT) FVIII

Outcome

FVIII thermal and chemical stability (rates of loss of FVIII activity at 57 °C or in guanidinium)surrogate

Altering contacts at the A1-C2 junction of Factor VIII by covalent modification or increasing hydrophobicity functionally enhances FVIII thermal stability.

Cite This Study

Wakabayashi et al. (2011) studied this question.

synapsesocial.com/papers/6a2113b201cd1e967e1e4025 https://doi.org/10.1074/jbc.m111.241109

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Increasing Hydrophobicity or Disulfide Bridging at the Factor VIII A1 and C2 Domain Interface Enhances Procofactor Stability

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Increasing Hydrophobicity or Disulfide Bridging at the Factor VIII A1 and C2 Domain Interface Enhances Procofactor Stability

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider