1 research outputs found
Optimal Interstrand Bridges for Collagen-like Biomaterials
In
some natural collagen triple helices, cysteine (Cys) residues
on neighboring strands are linked by disulfide bonds, enhancing association
and maintaining proper register. Similarly, Cys–Cys disulfide
bridges have been used to impose specific associations between collagen-mimetic
peptides (CMPs). Screening a library of disulfide linkers <i>in silico</i> for compatibility with collagen identifies the
disulfide bridge between proximal homocysteine (Hcy) and Cys as conferring
much greater stability than a Cys–Cys bridge, but only when
Hcy is installed in the Xaa position of the canonical Xaa–Yaa–Gly
repeat and Cys is installed in the Yaa position. Experimental evaluation
of CMPs that host alternative thiols validates this design: only Hcy-Cys
bridges improve triple-helical structure and stability upon disulfide-bond
formation. This privileged linker can enhance CMP-based biomaterials
and enable previously inaccessible molecular designs