Surface Chemistry is
an essential tool in
Protein and Peptide





Proteins and peptides expose surfaces
that behaves according to principles
known in Surface Chemistry.

In the human body, they interact
with cell surface components.
This interaction is determined by
specific and non- specific factors.

Before specific factors become active,
non-specific factors must already be
functioning. Peptides have to adsorb
at a target structure, and still be in an
active form, before they interact with it.

Surface Chemistry is hence one of the
essential disciplines in determining
protein and peptide activity.


  Information about release
of e.g. peptides can be found at

The membrane-binding C2 domain of Factor VIII
in presence of dodecylphosphocholine micelles
[1FAC - Veeraraghavan, S. et al., Biochem. J. 332
(1998) 549-555]. Image 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 above, the
membrane binding C2 domain of
Factor VIII is divided in hydrophilic
and hydrophobic regions.

The hydrophobic region is one key
factor in the membrane-binding
properties of the domain.

From the model it can be inferred that
in solution the large hydrophobic surface
will cause a more spherical shape
compared to the model, or alternatively, formation of di- or oligomer aggregates.

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