Covalent Capture of a Heterotrimeric Collagen Helix

Abstract

Stabilizing the three-dimensional structure of supramolecular materials can be accomplished through covalent capture of the assembled system. The lysine-aspartate charge pairs designed to direct the self-assembly of a collagen triple helix were subsequently used to covalently capture the helix through proximity-directed amide bond formation using EDC/HOBT activation. The triple helix thus stabilized maintains its folded structure and can now be used for applications previously inaccessible due to problematic folding equilibria.

Bioinspired photo-crosslinkable self-assembling peptides with pH-switchable “on–off” luminescence

“…Please do not adjust margins For instance, Hartgerink and his team reported the use of covalent capture of collagen mimetic peptides (CMPs), through the formation of isopeptide bonds between lysine and either aspartate or glutamate, using carboxylate activating reagents 1-ethyl-3-(3-(dimethylamino)propyl) carbodiimide (EDC) and Hydroxybenzotriazole (HOBt) [24,25]. By using a similar approach, our laboratory reported the design of covalent capture of SAPhydrogel using a one-pot in situ gelation system, based on EDC/Nhydroxysulfosuccinimide (sulfo-NHS) coupling, to readily cross-link LDLK12 molecules, in order to tune its biomechanics without affecting the spontaneous formation of β-sheet-containing nanofilaments [16].…”

Cross-Linked Self-Assembling Peptides and Their Post-Assembly Functionalization via One-Pot and In Situ Gelation System

“…Recently, our group pioneered the use of cross-linked peptide hydrogels with tuned and highly increased mechanical features suiting the needs of different regenerative medicine applications that, at the same time, effectively display bioactive motifs at their nanostructures [33,34]. Other groups have also utilized covalent capture to design more robust SAP-biomaterials under a variety of conditions [35][36][37]. However, these synthetic methods are relatively cumbersome and require long reaction times (up to 24 h).…”

Selective covalent capture of collagen triple helices with a minimal protecting group strategy

“…Alpha helical, 12 beta sheet [13][14][15][16][17] and polyproline type 2 secondary [18][19][20][21] structures have been prepared by this selfassembly followed by covalent capture approach.…”

“…Our group recently developed a covalent capture technique for collagen triple helices in which isopeptide bonds are formed between the side chains of lysine and aspartate or glutamate. [20][21][22] These engineered collagens were found to have improved thermal stability and an increased rate of folding while perfectly preserving the native triple helical fold of the assembled peptides.…”