Surface chemistry of
proteins and peptides
is one of the tools
needed in creation
of an active protein
formulation

Protein/Peptide
activity

 
     

EminTech 

 
         
   
 

In solution, proteins and peptides form
surfaces that behaves according to
principles known in surface chemistry.

Proteins interact with cell surfaces in vivo.
This interaction is determined by specific
and by non-specific factors.

Before the specific factors come into
play, the non-specific factors must be
taken care of.

Results from cooperation with
protein chemists at NOVO-Nordisk
and from consultant projects have
demonstrated that surface chemical
knowledge explains many effects
observed in protein and peptide
formulations
 


The membrane-binding C2 domain of Factor VIII
in presence of dodecylphosphocholine micelles
[1FAC - Veeraraghavan, S. et al., Biochem. J. 332
(1998) 549-555]. Images by Pymol.
 
   Amino acid color codes
  not polar, hydrophobic
  aromatic hydrophobic
  aromatic hydrophobic polar
  acidic (anionic)
  polar uncharged
  basic, (cationic)
  basic aromatic

 
As seen in the model, the membrane
binding C2 domain of Factor VIII show a
division in hydrophilic and hydrophobic
regions.

The hydrophobic region is probably
responsible for membrane-binding
properties of the domain.

The presence of the large hydrophobic
domain implies that the peptide either forms
a more spherical shape, or will aggregate
into di- or oligomers, in solution.

 
     
     
     
     
     
           
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