Covalent Capture of Collagen Triple Helices Using Lysine-Aspartate and Lysine-Glutamate Pairs.

Covalent Capture of Collagen Triple Helices Using Lysine-Aspartate and Lysine-Glutamate Pairs.
Biomacromolecules. 2020 Aug 21;:
Authors: Hulgan SAH, Jalan AA, Li IC, Walker DR, Miller MD, Kosgei AJ, Xu W, Phillips GN, Hartgerink JD
Abstract
Collagen mimetic peptides (CMPs) self-assemble into a triple helix reproducing the most fundamental aspect of the collagen structural hierarchy. They are therefore important for both further understanding this complex family of proteins and use in a wide range of biomaterials and biomedical applications. CMP self-assembly is complicated by a number of factors which limit the use of CMPs including their slow rate of folding, relatively poor monomer-trimer equilibrium, and the large number of competing species possible in heterotrimeric helices. All of these problems can be solved through the formation of isopeptide bonds between lysine and either aspartate or glutamate. These amino acids serve two purposes: they first direct self-assemble, allowing for composition and register control within the triple helix, and subsequently can be covalently linked, fixing the composition and register of the assembled structure without perturbing the triple helical conformation. This self-assembly and covalent capture are demonstrated here with four different triple helices. The formation of an isopeptide bond between lysine and glutamate (K-E) is shown to be a faster and higher yielding reaction than lysine with...

Source: Biomacromolecules - August 20, 2020 Category: Biochemistry Authors: Hulgan SAH, Jalan AA, Li IC, Walker DR, Miller MD, Kosgei AJ, Xu W, Phillips GN, Hartgerink JD Tags: Biomacromolecules Source Type: research