Newberry Robert W, VanVeller Brett, Raines Ronald T
Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706-1322, USA.
Chem Commun (Camb). 2015 Jun 14;51(47):9624-7. doi: 10.1039/c5cc02685g.
To probe noncovalent interactions within the collagen triple helix, backbone amides were replaced with a thioamide isostere. This subtle substitution is the first in the collagen backbone that does not compromise thermostability. A triple helix with a thioamide as a hydrogen bond donor was found to be more stable than triple helices assembled from isomeric thiopeptides.
为了探究胶原蛋白三螺旋内的非共价相互作用,主链酰胺被硫代酰胺等排体取代。这种细微的取代是胶原蛋白主链中的首次取代,且不会损害热稳定性。发现以硫代酰胺作为氢键供体的三螺旋比由异构硫肽组装而成的三螺旋更稳定。