Evidence map›Paper›PMID 30459362›Full record

ArticleScientific reports2018

C-Terminal Residue of Ultrashort Peptides Impacts on Molecular Self-Assembly, Hydrogelation, and Interaction with Small-Molecule Drugs.

Kiat Hwa Chan, Wei Hao Lee, Ming Ni, Yihua Loo, Charlotte A E Hauser

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 42 citations in OpenAlex.

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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

5 authors at 5 institutions in 4 countries.

Kiat Hwa ChanDivision of Science, Yale-NUS College, 16 College Avenue West, Singapore, 138527, Singapore. kiathwa.chan@yale-nus.edu.sg.
Wei Hao LeeDepartment of Chemistry, Krieger School of Arts & Sciences, 3400 North Charles Street, Johns Hopkins University, Baltimore, Maryland, USA.
Ming NiSchool of Biological Sciences & Engineering, Yachay Tech University, Hacienda San José s/n, San Miguel de Urcuquí, 100105, Ecuador.
Yihua LooInstitute of Bioengineering and Nanotechnology, 31 Biopolis Way, Singapore, 138669, Singapore.ORCID http://orcid.org/0000-0001-5211-7081
Charlotte A E HauserLaboratory for Nanomedicine, King Abdullah University of Science and Technology, Thuwal, 23955-6900, Saudi Arabia. charlotte.hauser@kaust.edu.sa.ORCID http://orcid.org/0000-0001-8251-7246
Institute of Bioengineering and Nanotechnology · SGJohns Hopkins University · USKing Abdullah University of Science and Technology · SAUniversidad Yachay Tech · ECYale-NUS College · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single molecular changes on a tripeptide can have dramatic effects on their self-assembly and hydrogelation. Herein, we explore C-terminal residue variation on two consistent ultrashort peptide backbones, i.e. acetylated-Leu-Ile-Val-Ala-Gly-Xaa and acetylated-Ile-Val-Xaa (Xaa = His, Arg, Asn). The objective of this study is to identify candidates that can form hydrogels for small-molecule drug (SMD) delivery. Haemolysis and cytotoxicity (with human adipose-derived mesenchymal stem cells) assays showed that the new soluble peptides (Xaa = His, Arg) are cytocompatible. Gelation studies showed that all but acetylated-Ile-Val-Arg could gel under physiological conditions. Longer peptidic backbones drive self-assembly more effectively as reflected in field emission scanning electron microscopy (FESEM) and circular dichroism spectroscopy studies. Rheological studies revealed that the resultant hydrogels have varying stiffness and yield stress, depending on the backbone and C-terminal residue. Visible spectroscopy-based elution studies with SMDs (naltrexone, methotrexate, doxorubicin) showed that besides the C-terminal residue, the shape of the SMD also determines the rate and extent of SMD elution. Based on the elution assays, infrared spectroscopy, and FESEM, we propose models for the peptide fibril-SMD interaction. Our findings highlight the importance of matching the molecular properties of the self-assembling peptide and SMD in order to achieve the desired SMD release profile.

Indexed as

AnimalsCircular DichroismDoxorubicinDrug CarriersDrug Delivery SystemsDrug LiberationHydrogelsMesenchymal Stem CellsMethotrexateMicroscopy, Electron, ScanningNaltrexoneNanostructuresPeptidesRabbitsRheologyStatic ElectricityDoxorubicinDrug CarriersHydrogelsMethotrexateNaltrexonePeptides

Identifiers

PMID30459362
PMCPMC6244206
OpenAlexW2900622933

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.