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Characterization of a synthetic peptide from the glycosaminoglycan binding site of heparin cofactor II

✍ Scribed by Herbert C. Whinna; Frank C. Church

Publisher
Springer Netherlands
Year
1994
Tongue
English
Weight
514 KB
Volume
1
Category
Article
ISSN
1573-3149

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✦ Synopsis

We characterized a synthetic peptide based on the glycosaminoglycan (GAG)-binding site of the serine proteinase inhibitor (serpin) heparin cofactor II (HCII): HCII'65-'9s, K'65DFVNASSKYEITTIHNLFRKLTHRLFRRNF'95. HCII'"5-195 negated acceleration of the HCII/thrombin inhibition reaction (IC, for the peptide shown in parentheses) by heparin (-250 nM) and dermatan sulfate (-500 nM). Circular dichroism spectra of HCII'65-'9s showed that GAGS increase the a-helical content of the peptide (percentage a-helix of the peptide/GAG complex given in parentheses): no GAG (7%) < low-molecular-weight heparin (32%) < heparin (42%) < dermatan sulfate (55%). A molecular model of HCII predicts that this region is 48% a-helix. Our results suggest: (i) HCI116s195 binds to GAGS; (ii) an a-helical conformation is preferable in the presence of GAGS; and (iii) GAGS may help stabilize a specific protein conformation in the HCII GAG-binding site, important for serpin function.

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