Evidence map›Paper›PMID 36137260›Full record

ArticleBiomacromolecules2022

Modulating Nanodroplet Formation En Route to Fibrillization of Amyloid Peptides with Designed Flanking Sequences.

Yanting Xing, Nicholas Andrikopoulos, Zhenzhen Zhang, Yunxiang Sun, Pu Chun Ke, Feng Ding

Open access · greenAbstract read
In one paragraph

Article in Biomacromolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 33% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. 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

6 authors at 4 institutions in 3 countries.

Yanting XingDepartment of Physics and Astronomy, Clemson University, Clemson, South Carolina 29634, United States.
Nicholas AndrikopoulosDrug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia.ORCID 0000-0001-8936-3534
Zhenzhen ZhangDepartment of Physics and Astronomy, Clemson University, Clemson, South Carolina 29634, United States.
Yunxiang SunDepartment of Physics and Astronomy, Clemson University, Clemson, South Carolina 29634, United States.ORCID 0000-0001-9799-7131
Pu Chun KeDrug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia.ORCID 0000-0003-2134-0859
Feng DingDepartment of Physics and Astronomy, Clemson University, Clemson, South Carolina 29634, United States.ORCID 0000-0003-1850-6336
Clemson University · USMonash University · AUNational Engineering Research Center for Nanotechnology · CNNingbo University · CN

Funding

Tissue Structural and Neural Remodeling in Human Sacroiliac JointP20GM121342 · NIGMS · CLEMSON UNIVERSITY · PI Hai Yao · 2018 to 2026
$24.7M
Inhibition of Human Islet Amyloid Polypeptide AggregationR35GM119691 · NIGMS · CLEMSON UNIVERSITY · PI DING, FENG · 2016 to 2020
$1.9M
NIGMS NIH HHS P20 GM121342NIGMS NIH HHS R35 GM119691
6 · The paper itself

Abstract

Soluble oligomers populating early amyloid aggregation can be regarded as nanodroplets of liquid-liquid phase separation (LLPS). Amyloid peptides typically contain hydrophobic aggregation-prone regions connected by hydrophilic linkers and flanking sequences, and such a sequence hydropathy pattern drives the formation of supramolecular structures in the nanodroplets and modulates subsequent fibrillization. Here, we studied LLPS and fibrillization of coarse-grained amyloid peptides with increasing flanking sequences. Nanodroplets assumed lamellar, cylindrical micellar, and spherical micellar structures with increasing peptide hydrophilic/hydrophobic ratios, and such morphologies governed subsequent fibrillization processes. Adding glycine-serine repeats as flanking sequences to Aβ

Indexed as

AmyloidAmyloidosisAmyloid beta-PeptidesGlycineHumansNanostructuresSerineAmyloidAmyloid beta-PeptidesGlycineSerine

Identifiers

PMID36137260
PMCPMC9618360
OpenAlexW4296806811

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.