Evidence map›Paper›PMID 39743532›Full record

ArticleJournal of nanobiotechnology2025

Facile universal strategy of presenting multifunctional short peptides for customizing desired surfaces.

Ruofei Lu, Bingyang Zhao, Kaiyuan Huo, Hao Liu, Yang Wang, Xingjie Zan, Siwang Hu

Abstract read
In one paragraph

Article in Journal of nanobiotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

7 authors.

Ruofei Lu *Department of Spinal Surgery, The First People's Hospital of Wenling, Affiliated Wenling Hospital, Wenzhou Medical University, Taizhou, Zhejiang, 317500, China.
Bingyang Zhao *School & Hospital of Stomatology, Wenzhou Medical University, Wenzhou, 325035, China.
Kaiyuan HuoWenzhou Institute, University of Chinese Academy of Sciences, Wenzhou Key Laboratory of Perioperative Medicine, Wenzhou, 325001, China.
Hao LiuSchool of Materials Science and Engineering, Zhengzhou University, Zhengzhou, 450001, China.
Yang WangWenzhou Institute, University of Chinese Academy of Sciences, Wenzhou Key Laboratory of Perioperative Medicine, Wenzhou, 325001, China. wangy0727@ucas.ac.cn.
Xingjie ZanWenzhou Institute, University of Chinese Academy of Sciences, Wenzhou Key Laboratory of Perioperative Medicine, Wenzhou, 325001, China. zanxj@ucas.ac.cn.
Siwang HuDepartment of Spinal Surgery, The First People's Hospital of Wenling, Affiliated Wenling Hospital, Wenzhou Medical University, Taizhou, Zhejiang, 317500, China. siwang_h@wmu.edu.cn.

Funding

Social Development Science and Technology Foundation of Taizhou 21ywb118Social Development Science and Technology Foundation of Wenling 2020S0180083startup funding from the Wenzhou Institute of UCAS WIUCASQD2019009startup funding from the Wenzhou Institute of UCAS WIUCASQD2021043Zhejiang Provincial Program for Medicine and Health 2022KY446
6 · The paper itself

Abstract

Interfacial properties determine biomaterial performances, such as cell adhesion, signal exchange, and biomineralization, which affect the tissue repair cycle and efficiency of clinical applications. Peptides, as short protein sequences that have defined functionalities, are highly stable and easy to synthesize and have enormous potential to reshape interfacial properties. However, the lack of a universal strategy for presenting peptides on various substrates substantially hinders the application of peptides. In this study, we report a facile and universal strategy for customizing desired interfacial functionalities by a well-known layer-by-layer (LbL) technique through the assembly polyphenols with positively charged short peptide-coupling functional sequences. Polyphenol-peptide interactions were elucidated in detail by assembling polyphenols and peptides possessing different characteristics (charged, uncharged, hydrophobic, and sequence length) in combination with molecular dynamics simulations, and isothermal titration calorimetry further revealed the favorable enthalpy change due to electrostatic interactions is the main driving force for assembling peptides with polyphenols. LbL coatings assembled from polyphenols and positively charged peptides exhibited good substrate generalization, stability, cell proliferation, and antioxidant properties, when prepared as hollow capsules by sacrificing the template, exhibited significant pH and ultrasound stimulation responses, which could be suitable candidates for drug carriers. Most importantly, the LbL assembly strategy of positively charged peptides could be utilized to present various functional molecules (such as arginyl-glycyl-aspartic acid (RGD), a cell adhesion motif; CM15, an antibacterial peptide; and PEG, an antifouling surface) on various substrates for customizing desired surfaces. This study not only provides new insights into the understanding and regulation of interactions between proteins/peptides and polyphenols but also paves the way toward the interfacial functionalization of biomaterials.

Indexed as

PeptidesPolyphenolsSurface PropertiesAnimalsAntioxidantsBiocompatible MaterialsCell AdhesionCell ProliferationHumansHydrophobic and Hydrophilic InteractionsMolecular Dynamics SimulationStatic ElectricityAntioxidantsBiocompatible MaterialsPeptidesPolyphenolsCustomized coatingLayer-by-layer assemblyPeptidePolyphenol

Identifiers

PMID39743532
PMCPMC11694446

What OpenQuestion holds

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LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.