Research Library

open-access-imgOpen AccessComprehensive multidimensional study of the self-assembly properties of a three residue substituted β 3 oligoamide
Buchanan Claire,
Hinds Mark G.,
Puskar Ljiljana,
Garvey Christopher J.,
Mechler Adam
Publication year2021
Publication title
pure and applied chemistry
Resource typeJournals
PublisherDe Gruyter
Substituted β 3 oligoamides form a unique self-assembling system where each monomer folds into a helix containing approximately three β 3 amino acids per turn, yielding a geometrically well-defined cylindrical building block that, when N-acylated, is able to self-assemble head-to-tail into nanorods that can reach several 100 μm length. It was shown in previous works that self-assembly can be achieved with a three residue long oligoamide as well that lacks any intramolecular H-bonds, yet it crystallizes in a helix-like conformation. The self-assembly properties of these small oligoamides are however elusive, suggesting a more complex system than the self-assembly of the H-bond stabilized helical monomers. Here we focus on the self-assembly behaviour of a three residue oligoamide, Ac-β 3 [LIA] where the letters denote the side chain of the analogous α amino acid. Ac-β 3 [LIA] can yield highly inhomogeneous suspensions in water with a broad range of large fibrous structures that seem to be very stable, yet occasionally fibre growth is only observed upon heating. The small size of the monomer suggests a highly dynamic equilibrium yet all previous attempts failed to clearly identify low molecular weight species. Therefore a special methodology was employed in this study to characterize the suspensions at different size ranges: SANS that is optimal to measure the small oligomers and cross sectional diameter of the assemblies, DLS that is sensitive to the large populations and therefore the length of the superstructures, and NMR that is sensitive to monomeric and small oligomeric form, in conjunction with IR spectroscopy to probe the folding and AFM to image the morphology of the assemblies. Temperature ramping was used to perturb the system to probe the dynamicity of the self-assembly. It was found that the anomalous self-assembly behaviour of Ac-β 3 [LIA] is caused by its two stable conformations, a helix-building “horseshoe” fold and a linear conformer. The latter is exclusively found in monomeric form in solution whereas the horseshoe fold is stable in solid phase and in fibrous assemblies. Small oligomers were absent. Thus the self-assembly of Ac-β 3 [LIA] is arrested by the activation energy need of the conformation change; fibre growth might be triggered by conditions that allow increased conformational freedom of the monomers. This observation may be used to develop strategies for controlled switchable self-assembly.
Subject(s)biology , chemistry , composite material , crystallography , ecology , helix (gastropod) , intramolecular force , materials science , monomer , organic chemistry , polymer , residue (chemistry) , self assembly , side chain , snail , stereochemistry , yield (engineering)
Keyword(s)14-helix, NICE 2020, β 3 peptides, spontaneous assembly, substituted oligoamides, temperature
SCImago Journal Rank0.439

Seeing content that should not be on Zendy? Contact us.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here