ArticleScience progress
The multifaceted helical net of amphipathic alpha-helices; the next dimension of the helical peptide wheel.
Article in Science progress. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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.
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.
Who cites it
2 citing papers in PubMed.
- Characterization of the pH-Dependent Stabilizing Forces of Insulin's Native and Fibril States.ACS physical chemistry Au · 2026Article
- α-Helical peptides: design strategies and recent advances in biomedical applications.Journal of translational medicine · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The amphipathic nature of helical proteins is crucial to their binding features across a broad spectrum of physiological examples, including heat-shock proteins and hyaluronic acid (HA) receptor binding. By taking advantage of the amphipathic balance of amino acids and their presentation in helical faces, novel synthetic peptides can be designed to improve biofunctionality. We present a new approach for designing synthetic alpha helical peptides using a multifaceted analysis, which allows for new bioengineering designs of amphipathic alpha helices. Amphipathic helical peptides were presented with distinct hydrophobic and hydrophilic faces; two series of analogs, namely, peptides AX9 and AX7, were designed to contain a hydrophobic and hydrophilic face, respectively. The presence of one series of peptides exhibited a distinct hydrophobic face and the second series exhibited a distinct hydrophilic face, which was corroborated with reversed-phase chromatography (C8). Using a multifaceted approach to analyze the potential faces of an amphipathic helix, we demonstrated that these helices contain seven distinct "side-viewed" helical faces (based on the hydrophobic face of the AXP series of analogs), which provides additional spatial dimensional information beyond the averaging effect of the hydrophobic moment generated from the "top-down" view of a helical wheel. Furthermore, we cross-compared our recently published HA-binding peptide in this manner to demonstrate that the most significant binding was related to (1) balanced amphipathicity and (2) a distribution of the key HA-binding domain B1(X
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.