Evidence map›Paper›PMID 36485036›Full record

ArticleMolecular pharmaceutics2023

Peptide Stability Is Important but Not a General Requirement for Antimicrobial and Antibiofilm Activity In Vitro and In Vivo.

Aaron P Decker, Yajuan Su, Biswajit Mishra, Atul Verma, Tamara Lushnikova, Jingwei Xie, Guangshun Wang

Open access · greenAbstract read
In one paragraph

Article in Molecular pharmaceutics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

6 citing papers in PubMed, 11 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

7 authors at 1 institution in 1 country.

Aaron P DeckerDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, 985900 Nebraska Medical Center, Omaha, Nebraska 68198-5900, United States.
Yajuan SuDepartment of Surgery-Transplant and Mary & Dick Holland Regenerative Medicine Program, College of Medicine, University of Nebraska Medical Center, Omaha, Nebraska 68198, United States.
Biswajit MishraDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, 985900 Nebraska Medical Center, Omaha, Nebraska 68198-5900, United States.
Atul VermaDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, 985900 Nebraska Medical Center, Omaha, Nebraska 68198-5900, United States.
Tamara LushnikovaDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, 985900 Nebraska Medical Center, Omaha, Nebraska 68198-5900, United States.
Jingwei XieDepartment of Surgery-Transplant and Mary & Dick Holland Regenerative Medicine Program, College of Medicine, University of Nebraska Medical Center, Omaha, Nebraska 68198, United States.ORCID 0000-0002-8126-1397
Guangshun WangDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, 985900 Nebraska Medical Center, Omaha, Nebraska 68198-5900, United States.ORCID 0000-0002-4841-7927
University of Nebraska Medical Center · US

Funding

Novel Janus-type Antimicrobial Dressings for the Treatment of Biofilms in Chronic WoundsR01GM138552 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI WANG, GUANGSHUN, XIE, JINGWEI · 2020 to 2023
$2.2M
NIGMS NIH HHS R01 GM138552
6 · The paper itself

Abstract

Peptide stability to proteases has been a major requirement for developing peptide therapeutics. This study investigates the effects of peptide stability on antimicrobial and antibiofilm activity under various conditions. For this purpose, two human cathelicidin-derived peptides differing in stability to proteases were utilized. While GF-17, a peptide derived from the major antimicrobial region of human LL-37, can be rapidly cleaved by proteases, the engineered peptide 17BIPHE2 is resistant to multiple proteases. In the standard antimicrobial susceptibility, killing kinetics, and membrane permeabilization assays conducted in vitro using planktonic bacteria, these two peptides displayed similar potency. The two peptides were also similarly active against methicillin-resistant

Indexed as

Anti-Infective AgentsMethicillin-Resistant Staphylococcus aureusAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBiofilmsHumansMiceMicrobial Sensitivity TestsPeptide HydrolasesAnti-Bacterial AgentsAnti-Infective AgentsAntimicrobial Cationic PeptidesPeptide Hydrolasesantimicrobial susceptibilitybiofilmsLL-37MRSApeptide stabilitywound healing

Identifiers

PMID36485036
PMCPMC12766539
OpenAlexW4310943238

What OpenQuestion holds

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LicenceTDM
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.