Sequence-Directed Hierarchyof Supramolecular PeptideBilayers and Heme Cofactor Insertion

Jesse L. Prelesnik; Andrew Lau; Nathan C. Laud; Kelsie J. Li; Yuzi Liu; Henry Chan; H. Christopher Fry

doi:10.1021/jacs.6c05871

August 17, 2026Journal of the American Chemical Society

Sequence-Directed Hierarchyof Supramolecular PeptideBilayers and Heme Cofactor Insertion

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Key Points

To investigate how peptide sequence variations that modify hydrophobicity and charge–charge repulsion control bilayer assembly, stability, and heme cofactor uptake.
Combined wet-lab experiments with molecular dynamics simulations using a series of representative amphiphilic peptides (ExL4–xL5HL6 for x = 2, 3, 4).
Characterized nanoscale self-assembly, membrane compressibility, permeability, stability, and cofactor sequestration efficiency across sequence variations.
Single-residue sequence alterations substantially modified aggregate morphology, stability, and heme binding capacity.
Increased membrane permeability and compressibility enhanced heme uptake but required a strict trade-off with overall bilayer structural stability.

Implication

Experimental and computational analysis reveals how sequence variations govern heme uptake and stability in supramolecular peptide bilayers, highlighting key trade-offs in biomaterial design.

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Cite This Study

Prelesnik et al. (2026) studied this question.

synapsesocial.com/papers/6a85643903308d306e2d7e1e https://doi.org/10.1021/jacs.6c05871

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Sequence-Directed Hierarchyof Supramolecular PeptideBilayers and Heme Cofactor Insertion

Key Points

Implication

Abstract

Discussion

Cite This Study

Sequence-Directed Hierarchyof Supramolecular PeptideBilayers and Heme Cofactor Insertion

Key Points

Implication

Abstract

Discussion

Cite This Study

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