Chemical synthesis and evaluation of a backbone-cyclized minimized 2-helix Z-domain

QC 20110615
The Z-molecule is a small, engineered IgG-binding affinity protein derived from the immunoglobulin-binding domain B of Staphylococcus aureus protein A. The Z-domain consists of 58 amino acids forming a well-defined antiparallel three-helix structure. Two of the three helices are involved in ligand binding, whereas the third helix provides structural support to the three-helix bundle. The small size and the stable three-helix structure are two attractive properties comprised in the Z-domain, but a further reduction in size of the protein is valuable for several reasons. Reduction in size facilitates synthetic production of any protein-based molecule, which is beneficial from an economical viewpoint. In addition, a smaller protein is easier to manipulate through chemical modifications. By omitting the third stabilizing helix from the Z-domain and joining the N- and C-termini by a native peptide bond, the affinity protein obtains the advantageous properties of a smaller scaffold and in addition becomes resistant to exoproteases. We here demonstrate the synthesis and evaluation of a novel cyclic two-helix Z-domain. The molecule has retained affinity for its target protein, is resistant to heat treatment, and lacks both N- and C-termini. Copyright (C) 2011 European Peptide Society and John Wiley & Sons, Ltd.

NATURVETENSKAP Biologi Biokemi och molekylärbiologi hsv//swe
NATURAL SCIENCES Biological Sciences Biochemistry and Molecular Biology hsv//eng
protein scaffold
Z-domain
two-helix protein
SPPS
IgG
affinity purification
Molecular biology
Molekylärbiologi

Mikaelsson, CeciliaKTH,Molekylär Bioteknologi(Swepub:kth)u1bla3bl (författare)
Karlstrom Eriksson, AmelieKTH,Molekylär Bioteknologi(Swepub:kth)u10x6l4n (författare)
KTHMolekylär Bioteknologi (creator_code:org_t)

Av författaren/redakt...: Järver, Peter; Mikaelsson, Ceci ...; Karlstrom Erikss ...

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