Evidence map›Paper›PMID 36012300›Full record

ReviewInternational journal of molecular sciences2022

Membrane Internalization Mechanisms and Design Strategies of Arginine-Rich Cell-Penetrating Peptides.

Minglu Hao, Lei Zhang, Pu Chen

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
7.0field-weighted citation impact, top 2% of its field
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

49 citing papers in PubMed, 92 citations in OpenAlex.

  1. Review
  2. Article
  3. Self-Assembling Short Peptide Carriers for Gene Delivery.International journal of molecular sciences · 2026
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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

3 authors at 2 institutions in 2 countries.

Minglu HaoAdvanced Materials Institute, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250014, China.
Lei ZhangDepartment of Chemical Engineering, Waterloo Institute for Nanotechnology, University of Waterloo, 200 University Avenue West, Waterloo, ON N2L3G1, Canada.ORCID 0000-0001-5454-8758
Pu ChenAdvanced Materials Institute, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250014, China.
University of Waterloo · CAQilu University of Technology · CN

Funding

Innovation Pilot Project of Integration of Science, Education and Industry of Shandong Province 2020KJC-CG04Mitacs IT18262
6 · The paper itself

Abstract

Cell-penetrating peptides (CPPs) have been discovered to deliver chemical drugs, nucleic acids, and macromolecules to permeate cell membranes, creating a novel route for exogenous substances to enter cells. Up until now, various sequence structures and fundamental action mechanisms of CPPs have been established. Among them, arginine-rich peptides with unique cell penetration properties have attracted substantial scientific attention. Due to the positively charged essential amino acids of the arginine-rich peptides, they can interact with negatively charged drug molecules and cell membranes through non-covalent interaction, including electrostatic interactions. Significantly, the sequence design and the penetrating mechanisms are critical. In this brief synopsis, we summarize the transmembrane processes and mechanisms of arginine-rich peptides; and outline the relationship between the function of arginine-rich peptides and the number of arginine residues, arginine optical isomers, primary sequence, secondary and ternary structures, etc. Taking advantage of the penetration ability, biomedical applications of arginine-rich peptides have been refreshed, including drug/RNA delivery systems, biosensors, and blood-brain barrier (BBB) penetration. Understanding the membrane internalization mechanisms and design strategies of CPPs will expand their potential applications in clinical trials.

Indexed as

Cell-Penetrating PeptidesArginineBiological TransportCell MembraneDrug Delivery SystemsArginineCell-Penetrating Peptidesarginine-rich peptidebiomedical applicationsCPPsmechanism of internalizationnon-covalent interactionpeptide design

Identifiers

PMID36012300
PMCPMC9409441
OpenAlexW4291465184

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.