Molecular Insight into the β‑Sheet Twist and Related Morphology of Self-Assembled Peptide Amphiphile Ribbons
journal contributionposted on 2021-11-11, 20:03 authored by Qinsi Xiong, Samuel I. Stupp, George C. Schatz
Self-assembly of high-aspect-ratio filaments containing β-sheets has attracted much attention due to potential use in bioengineering and biomedicine. However, precisely predicting the assembled morphologies remains a grand challenge because of insufficient understanding of the self-assembly process. We employed an atomistic model to study the self-assembly of peptide amphiphiles (PAs) containing valine–glutamic acid (VE) dimeric repeats. By changing of the sequence length, the assembly morphology changes from flat ribbon to left-handed twisted ribbon, implying a relationship between β-sheet twist and strength of interstrand hydrogen bonds. The calculations are used to quantify this relationship including both magnitude and sign of the ribbon twist angle. Interestingly, a change in chirality is observed when we introduce the RGD epitope into the C-terminal of VE repeats, suggesting arginine and glycine’s role in suppressing right-handed β-sheet formation. This study provides insight into the relationship between β-sheet twist and self-assembled nanostructures including a possible design rule for PA self-assembly.
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possible design ruleinterstrand hydrogen bondsassembled morphologies remainsassembled nanostructures includingribbon twist anglehanded twisted ribbonstudy provides insightassembly morphology changesflat ribbonsheet twistrelated morphologymolecular insightsuppressing rightsuggesting argininesheet formationsequence lengthrgd epitoperelationship includingprecisely predictingpotential usepeptide amphiphilesinsufficient understandinghanded βgrand challengeglycine ’atomistic modelassembly process