Evidence map›Paper›PMID 40597991›Full record

ArticleBMC biotechnology2025

Central position of histidine in the sequence of designed alternating polarity peptides enhances pH-responsive assembly with DNA.

Razieh Taghizadeh Pirposhteh, Nasir Mohajel, Arash Arashkia, Kayhan Azadmanesh, Mohammadali Masoumi

Abstract read
In one paragraph

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

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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

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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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Razieh Taghizadeh PirposhtehDepartment of Molecular Virology, Pasteur Institute of Iran, 12th Farvardin St., Tehran, 1316943551, Iran.
Nasir MohajelDepartment of Molecular Virology, Pasteur Institute of Iran, 12th Farvardin St., Tehran, 1316943551, Iran. nasirmohajel@gmail.com.
Arash ArashkiaDepartment of Molecular Virology, Pasteur Institute of Iran, 12th Farvardin St., Tehran, 1316943551, Iran.
Kayhan AzadmaneshDepartment of Molecular Virology, Pasteur Institute of Iran, 12th Farvardin St., Tehran, 1316943551, Iran.
Mohammadali MasoumiDepartment of Molecular Virology, Pasteur Institute of Iran, 12th Farvardin St., Tehran, 1316943551, Iran.

Funding

the Iran National Science Foundation (INSF) 97011564
6 · The paper itself

Abstract

backgroundSelf-assembling peptides hold great promise for medical applications, particularly as carriers for gene delivery, but their potential remains unrealized due to a limited understanding of how amino acid sequence positioning affects their properties. In this study, we designed and evaluated two alternating polarity peptides, RFH (RFRHRHRFR) and RHF (RHRFRFRHR), differing only in the position of their histidine and phenylalanine residues, to investigate the impact of sequence variation on pH-responsive DNA co-assembly and transfection efficiency.

resultsBoth peptides formed stable co-assemblies with DNA at neutral pH. However, RHF retained its co-assembling ability at acidic pH, as confirmed by gel retardation studies. Coarse-grained molecular dynamics simulations further supported these findings, showing a reduced affinity of RFH for DNA and a sharper decrease in DNA binding when its histidine residues were protonated. Morphological analysis revealed that both co-assemblies underwent structural transitions with increasing N/P ratios, though their sizes and morphologies differed significantly. Biological studies demonstrated that both peptides achieved a higher transfection efficiency in 293T and HeLa cells compared to R

conclusionsThese findings highlight the importance of histidine positioning within peptide sequences for tuning pH-responsiveness and optimizing DNA co-assembly and transfection efficiency. The results provide valuable insights for the rational design of efficient, safe, and pH-responsive peptide-based gene delivery systems.

Indexed as

DNAHistidinePeptidesAmino Acid SequenceHEK293 CellsHeLa CellsHumansHydrogen-Ion ConcentrationMolecular Dynamics SimulationTransfectionDNAHistidinePeptidesAlternating polarityAmphiphilic peptidesCoarse-grained molecular dynamics simulationNonviral gene deliveryPH-responsiveSelf-assembling peptides

Identifiers

PMID40597991
PMCPMC12210498

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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.