From the journal:

Chemical Communications

Fluorine-induced helical assembly of dipeptides and its remote magnetic alignment

Chaoyi Zhu,†ab   Jixiang Ni,†ab   JianXun Shen, ORCID logo c   Haotian Mao, ORCID logo d   Yang Lu, ORCID logo *ab   Jianxi Ying, ORCID logo *ab   Ning Xi*ab  and  Yufen Zhao ORCID logo ab  

* Corresponding authors

a Institute of Drug Discovery Technology (IDDT), Ningbo University, Ningbo 315211, China

b Qian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences, Ningbo University, Ningbo 315211, China

c Key Laboratory of Planetary Science and Frontier Technology, Institute of Geology and Geophysics, Chinese Academy of Sciences, Beijing 100029, China

d Hubei Key Laboratory of Planetary Geology and Deep Space Exploration, School of Earth and Planetary Sciences, China University of Geosciences, Wuhan 430074, China

Abstract

2,6-Difluorination alters the supramolecular packing of a lactam–phenylalanine dipeptide, changing the non-fluorinated lamellar arrangement into a compact helical packing architecture. The resulting assemblies exhibit enhanced magnetic-field-assisted orientation during deposition and drying.

Graphical abstract: Fluorine-induced helical assembly of dipeptides and its remote magnetic alignment

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Article information

DOI
https://doi.org/10.1039/D6CC02008A
Article type
Communication
Submitted
01 Apr 2026
Accepted
02 Jun 2026
First published
03 Jun 2026

Chem. Commun., 2026, Advance Article

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Fluorine-induced helical assembly of dipeptides and its remote magnetic alignment

C. Zhu, J. Ni, J. Shen, H. Mao, Y. Lu, J. Ying, N. Xi and Y. Zhao, Chem. Commun., 2026, Advance Article , DOI: 10.1039/D6CC02008A

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