Evidence map›Paper›PMID 29403673›Full record

ArticleFrontiers of chemical science and engineering2017

Enzyme-Instructed Self-Assembly of Peptides Containing Phosphoserine to Form Supramolecular Hydrogels as Potential Soft Biomaterials.

Jie Zhou, Xuewen Du, Jiaqing Wang, Natsuko Yamagata, Bing Xu

Open access · greenAbstract read
In one paragraph

Article in Frontiers of chemical science and engineering, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

12 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Enzymatic Noncovalent Synthesis.Chemical reviews · 2020
    Review
  10. Review
  11. Article
  12. Enzymatic Control of the Conformational Landscape of Self-Assembling Peptides.Angewandte Chemie (International ed. in English) · 2018
    Article
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

5 authors at 1 institution in 1 country.

Jie ZhouDepartment of Chemistry, Brandeis University, 415 South St., Waltham, MA, 02453, USA.
Xuewen DuDepartment of Chemistry, Brandeis University, 415 South St., Waltham, MA, 02453, USA.
Jiaqing WangDepartment of Chemistry, Brandeis University, 415 South St., Waltham, MA, 02453, USA.
Natsuko YamagataDepartment of Chemistry, Brandeis University, 415 South St., Waltham, MA, 02453, USA.
Bing XuDepartment of Chemistry, Brandeis University, 415 South St., Waltham, MA, 02453, USA.
Brandeis University · US

Funding

Subcellular Enzyme-instructed self-assembly for molecular anticancer nanomedicinesR01CA142746 · NCI · BRANDEIS UNIVERSITY · PI Bing Xu · 2010 to 2026
$6.4M
NCI NIH HHS R01 CA142746
6 · The paper itself

Abstract

Enzyme-instructed self-assembly (EISA) offers a facile approach to explore the supramolecular assemblies of small molecules in cellular milieu for a variety of biomedical applications. One of the commonly used enzymes is phosphatase, but the study of the substrates of phosphatases mainly focuses on the phosphotyrosine containing peptides. In this work, we examine the EISA of phosphoserine containing small peptides for the first time by designing and synthesizing a series of precursors containing only phosphoserine or both phosphoserine and phosphotyrosine. Conjugating a phosphoserine to the C-terminal of a well-established self-assembling peptide backbone, (naphthalene-2-ly)-acetyl-diphenylalanine (NapFF), affords a novel hydrogelation precursor for EISA. The incorporation of phosphotyrosine, another substrate of phosphatase, into the resulting precursor, provides one more enzymatic trigger on a single molecule, and meanwhile increases the precursors' propensity to aggregate after being fully dephosphorylated. Exchanging the positions of phosphorylated serine and tyrosine in the peptide backbone provides insights on how the specific molecular structures influence self-assembling behaviors of small peptides and the subsequent cellular responses. Moreover, the utilization of D-amino acids largely enhances the biostability of the peptides, thus providing a unique soft material for potential biomedical applications.

Indexed as

Enzyme-instructed self-assemblyphosphatasephosphoserinesupramolecular hydrogel

Identifiers

PMID29403673
PMCPMC5796776
OpenAlexW2572949890

What OpenQuestion holds

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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.