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Showing 1–7 of 7 results

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Publisher Correction: Assembly of short amphiphilic peptoids into nanohelices with controllable supramolecular chirality

Renyu Zheng
Mingfei Zhao
Chun-Long Chen
Amendments and CorrectionsOpen Access03 Sept 2025
Nature Communications

Volume: 16, P: 1
Author Correction: Antiviral fibrils of self-assembled peptides with tunable compositions

Joseph Dodd-o
Abhishek Roy
Vivek Kumar
Amendments and CorrectionsOpen Access28 Aug 2024
Nature Communications

Volume: 15, P: 1
Antiviral fibrils of self-assembled peptides with tunable compositions

In this work, the authors report the use of a computationally and rationally designed self-assembling peptide that has robust antiviral capability with demonstrated specificity in binding to SARS-CoV-2 and inhibition of viral entry into human cells.

Joseph Dodd-o
Abhishek Roy
Vivek Kumar
ResearchOpen Access07 Feb 2024
Nature Communications

Volume: 15, P: 1-14
Author Correction: Antiviral fibrils of self-assembled peptides with tunable compositions

Joseph Dodd-o
Abhishek Roy
Vivek Kumar
Amendments and CorrectionsOpen Access19 Feb 2024
Nature Communications

Volume: 15, P: 1
Assembly of short amphiphilic peptoids into nanohelices with controllable supramolecular chirality

Helical protein assemblies are an important biological structure, but are challenging to mimic with synthetic materials. Here, the authors report the use of peptoids to form nanohelix structures with controllable supramolecular chirality.

Renyu Zheng
Mingfei Zhao
Chun-Long Chen
ResearchOpen Access16 Apr 2024
Nature Communications

Volume: 15, P: 1-9
A common pathway for detergent-assisted oligomerization of Aβ42

A study jointly using solid-state NMR spectroscopy and molecular dynamics simulations reveals a common pathway for the detergent-assisted oligomerization of Aβ42.

Fidha Nazreen Kunnath Muhammedkutty
Ramesh Prasad
Huan-Xiang Zhou
ResearchOpen Access21 Nov 2023
Communications Biology

Volume: 6, P: 1-10
Charge guides pathway selection in β-sheet fibrillizing peptide co-assembly

Co-assembly of peptide mixtures can yield interesting materials, but predictive understanding of assembly pathways is lacking. Here the self- and co-assembly preferences of oppositely-charged peptides are systematically studied experimentally and by molecular dynamics simulations.

Dillon T. Seroski
Xin Dong
Gregory A. Hudalla
ResearchOpen Access13 Nov 2020
Communications Chemistry

Volume: 3, P: 1-11