Bacterial collagen-binding domain targets undertwisted regions of collagen.

ABSTRACT: Clostridium histolyticum collagenase causes extensive degradation of collagen in connective tissue that results in gas gangrene. The C-terminal collagen-binding domain (CBD) of these enzymes is the minimal segment required to bind to a collagen fibril. CBD binds unidirectionally to the undertwisted C-terminus of triple helical collagen. Here, we examine whether CBD could also target undertwisted regions even in the middle of the triple helix. Collageneous peptides with an additional undertwisted region were synthesized by introducing a Gly → Ala substitution [(POG)(x) POA(POG)(y)]₃, where x + y = 9 and x > 3). ¹H-¹⁵N heteronuclear single quantum coherence nuclear magnetic resonance (HSQC NMR) titration studies with ¹⁵N-labeled CBD demonstrated that the minicollagen binds to a 10 Å wide 25

SUBMITTER: Philominathan ST 

PROVIDER: S-EPMC3526996 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature