Evidence map›Paper›PMID 32224438›Full record

ArticleJournal of chromatography. B, Analytical technologies in the biomedical and life sciences2020

Quantification of residual hydrophobic fusion peptide with monomer and dimer forms using reversed-phase liquid chromatography.

Cindy X Cai, Nicole A Schneck, Vera B Ivleva, Krishana Gulla, Yaqiu Zhang, Daniel Gowetski, Q Paula Lei

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 51% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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 2 institutions in 1 country.

Cindy X CaiVaccine Production Program Laboratory, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Gaithersburg, MD, United States.
Nicole A SchneckVaccine Production Program Laboratory, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Gaithersburg, MD, United States.
Vera B IvlevaVaccine Production Program Laboratory, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Gaithersburg, MD, United States.
Krishana GullaVaccine Production Program Laboratory, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Gaithersburg, MD, United States.
Yaqiu ZhangVaccine Production Program Laboratory, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Gaithersburg, MD, United States.
Daniel GowetskiVaccine Production Program Laboratory, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Gaithersburg, MD, United States.
Q Paula LeiVaccine Production Program Laboratory, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Gaithersburg, MD, United States. Electronic address: paula.lei@nih.gov.
National Institutes of Health · USNational Institute of Allergy and Infectious Diseases · US

Funding

Intramural NIH HHS Z99 AI999999
6 · The paper itself

Abstract

A fusion peptide mimicking a part of the sequence of HIV-1 envelope glycoprotein with an additional cysteine at its C-terminus (FP8: AVGIGAVFC) was conjugated to a carrier protein through a linker for development of an HIV-1 vaccine. Since this fusion peptide is very hydrophobic with poor solubility and can self-dimerize via a disulfide bond, co-existence of monomeric and dimeric forms presented a major challenge for residual unconjugated FP8 quantification. A reversed-phase liquid chromatography (RPLC) with UV detection was developed to monitor residual FP8 using an experimental correction factor of 0.85 for UV peak area measurement between FP8 dimer and monomer. Therefore, both forms of unconjugated residual FP8 can be measured based on a single FP8 monomer reference curve. Overall, this study demonstrated that the current purification process can remove free residual FP8 to a low level, <20 µg/mL, which showed negligible impact (<10%) for the conjugated FP8 ratio measurement using another method, amino acid analysis.

Indexed as

Amino Acid SequenceChromatography, High Pressure LiquidChromatography, Reverse-PhaseCysteineDisulfidesHumansHydrophobic and Hydrophilic InteractionsLimit of DetectionPeptidesProtein ConformationProtein MultimerizationRecombinant Fusion ProteinsCysteineDisulfidesPeptidesRecombinant Fusion ProteinsDimerFusion peptideHIV-1 vaccineMonomerPeptide quantificationReversed-phase liquid chromatography

Identifiers

PMID32224438
PMCPMC8138758
OpenAlexW3012244514

What OpenQuestion holds

Textmetadata
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.