Evidence map›Paper›PMID 40362238›Full record

ReviewInternational journal of molecular sciences2025

Probing Peptide Assembly and Interaction via High-Resolution Imaging Techniques: A Mini Review.

Xiaoming Zhang, Zhanshu Yang, Jiaxuan Lin, Wei Zhou, Nan Sun, Yi Jia

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Xiaoming ZhangSchool of Science, Minzu University of China, Beijing 100081, China.ORCID 0000-0001-8707-9097
Zhanshu YangSchool of Science, Minzu University of China, Beijing 100081, China.
Jiaxuan LinSchool of Science, Minzu University of China, Beijing 100081, China.
Wei ZhouSchool of Science, Minzu University of China, Beijing 100081, China.
Nan SunNational Engineering Research Center for Colloidal Materials, School of Chemistry and Chemical Engineering, Shandong University, Jinan 250100, China.
Yi JiaBeijing National Laboratory for Molecular Sciences, CAS Key Laboratory of Colloid, Interface and Chemical Thermodynamics, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100190, China.ORCID 0000-0001-9812-667X

Funding

the Hubei Key Laboratory of Novel Reactor and Green Chemical Technology No. NRG202414the National Natural Science Foundation of China No. 12174462the Natural Science Foundation of Shandong Province No. ZR2024QB312
6 · The paper itself

Abstract

Peptide molecules, as fundamental structural units in biological systems, play pivotal roles in diverse biological processes and have garnered substantial attention in biomolecular self-assembly research. Their structural simplicity and high design flexibility make peptides key players in the development of novel biomaterials. High-resolution imaging techniques have provided profound insights into peptide assembly. Recently, the development of cutting-edge technologies, such as super-resolution microscopy (SRM) with unparalleled spatiotemporal resolution, has further advanced peptide assembly research. These advancements enable both the mechanistic exploration of peptide assembly pathways and the rational design of peptide-based functional materials. In this mini review, we systematically examine the structural diversity of peptide assemblies, including micelles, tubes, particles, fibers and hydrogel, as investigated by various high-resolution imaging techniques, with a focus on their assembly characterization and dynamic process. We also summarize the interaction networks of peptide assemblies with proteins, polymers and microbes, providing further insight into the interactions between peptide assemblies and other molecules. Furthermore, we emphasize the transformative role of high-resolution imaging techniques in addressing long-standing challenges in peptide nanotechnology. We anticipate that this review will accelerate the advancement of peptide assembly characterization, thereby fostering the creation of next-generation functional biomaterials.

Indexed as

PeptidesBiocompatible MaterialsHumansHydrogelsMicellesNanotechnologyBiocompatible MaterialsHydrogelsMicellesPeptidesbiomaterialsnanotechnologypeptide moleculesself-assemblysuper-resolution microscopy

Identifiers

PMID40362238
PMCPMC12071768

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.