Evidence map›Paper›PMID 31159194›Full record

ArticleMolecules (Basel, Switzerland)2019

Novel pH Selective, Highly Lytic Peptides Based on a Chimeric Influenza Hemagglutinin Peptide/Cell Penetrating Peptide Motif.

Bethany Algayer, Ann O'Brien, Aaron Momose, Dennis J Murphy, William Procopio, David M Tellers, Thomas J Tucker

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. A Novel Cell-Penetrating Lipopeptide for DNA Binding, Self-Assembly, and Delivery Into HeLa and Pluripotent Stem Cells.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Coiled coil exposure and histidine tags drive function of an intracellular protein drug carrier.Journal of controlled release : official journal of the Controlled Release Society · 2021
    Article
  9. 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 at 1 institution in 1 country.

Bethany AlgayerMerck Research Laboratories, Merck and Co, Inc., West Point, PA 19486, USA. bethany_algayer@merck.com.
Ann O'BrienMerck Research Laboratories, Merck and Co, Inc., West Point, PA 19486, USA. aobrien@incyte.com.
Aaron MomoseMerck Research Laboratories, Merck and Co, Inc., West Point, PA 19486, USA. aam888010@icloud.com.
Dennis J MurphyMerck Research Laboratories, Merck and Co, Inc., West Point, PA 19486, USA. dennis.murphy@merck.com.
William ProcopioMerck Research Laboratories, Merck and Co, Inc., West Point, PA 19486, USA. wmprocop@gmail.com.
David M TellersMerck Research Laboratories, Merck and Co, Inc., West Point, PA 19486, USA. david_tellers@merck.com.
Thomas J TuckerMerck Research Laboratories, Merck and Co, Inc., West Point, PA 19486, USA. tom_tucker@merck.com.
United States Military Academy · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Delivery of macromolecular cargos such as siRNA to the cytosol after endocytosis remains a critical challenge. Numerous approaches including viruses, lipid nanoparticles, polymeric constructs, and various peptide-based approaches have yet to yield a general solution to this delivery issue. In this manuscript, we describe our efforts to design novel endosomolytic peptides that could be used to facilitate the release of cargos from a late endosomal compartment. These amphiphilic peptides, based on a chimeric influenza hemagglutinin peptide/cell-penetrating peptide (CPP) template, utilize a pH-triggering mechanism in which the peptides are protonated after acidification of the endosome, and thereby adopt an alpha-helical conformation. The helical forms of the peptides are lytically active, while the non-protonated forms are much less or non-lytically active at physiological pH. Starting from an initial lead peptide (INF7-Tat), we systematically modified the sequence of the chimeric peptides to obtain peptides with greatly enhanced lytic activity that maintain good pH selectivity in a red blood cell hemolysis assay.

Indexed as

Amino Acid MotifsCell-Penetrating PeptidesHemagglutinin Glycoproteins, Influenza VirusHydrogen-Ion ConcentrationAmino Acid SequenceCircular DichroismHemolysisHumansProteolysisSpectrum AnalysisCell-Penetrating PeptidesHemagglutinin Glycoproteins, Influenza Virusamphiphilicendosomolyticfusogenicinfluenza hemagglutininpeptidesRBC lysis

Identifiers

PMID31159194
PMCPMC6600388
OpenAlexW2947461501

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.