Multivalent Protein Assembly Using Monovalent Self-Assembling Building Blocks

Abstract

Discotic molecules, which self-assemble in water into columnar supramolecular polymers, emerged as an alternative platform for the organization of proteins. Here, a monovalent discotic decorated with one single biotin was synthesized to study the self-assembling multivalency of this system in regard to streptavidin. Next to tetravalent streptavidin, monovalent streptavidin was used to study the protein assembly along the supramolecular polymer in detail without the interference of cross-linking. Upon self-assembly of the monovalent biotinylated discotics, multivalent proteins can be assembled along the supramolecular polymer. The concentration of discotics, which influences the length of the final polymers at the same time dictates the amount of assembled proteins.

Facilitating functionalization of benzene-1,3,5-tricarboxamides by switching amide connectivity

“…15 Finally, the periphery of various columnar structures formed by discotic molecules were decorated with carbohydrates to trigger cellular uptake 16,17 and with biotin to create a fibrous scaffold for protein binding. 18,19 The self-assembly of discotic benzene-1,3,5-tricarboxamides (BTAs) into supramolecular polymers has been studied extensively in recent years. 20 The amides can be connected to the benzene ring via the carbonyl group or via the nitrogen atom, yielding C-centred and N-centred BTAs, respectively.…”

“…15 Finally, the periphery of various columnar structures formed by discotic molecules were decorated with carbohydrates to trigger cellular uptake 16,17 and with biotin to create a fibrous scaffold for protein binding. 18,19 …”

Multivalent Noncovalent Interfacing and Cross‐Linking of Supramolecular Tubes

“…Interaction between biotin and SAv that can be codissolved in the solution provides highly specific and strong interaction [ 23 ] which has already been employed for the analysis of interaction of biotinylated amphiphilic peptides with avidin [ 24 ] and for templating protein assembly by supramolecular fibers. [ 25 ] Furthermore, SAv‐coated surfaces and interfacing platforms have been previously reported, [ 26 ] while SAv itself has high stability when complexed with biotins. [ 27,28 ]…”

Infinite Assembly of Folded Proteins in Evolution, Disease, and Engineering

“…They created a linear ligand with biotin groups that dimerized through coordination bonds to iron(II), thus leading to one‐dimensional assembly, the formation of which was dependent on the presence of iron . In a different approach, Brunsveld and co‐workers used a ligand capable of stacking into filaments and showed it could act as a scaffold for proteins by way of its appended biotin moieties …”