Evidence map›Paper›PMID 25251904›Full record

ArticleBiomacromolecules2014

Engineering complementary hydrophobic interactions to control β-hairpin peptide self-assembly, network branching, and hydrogel properties.

Sameer Sathaye, Huixi Zhang, Cem Sonmez, Joel P Schneider, Christopher M MacDermaid, Christopher D Von Bargen, Jeffery G Saven, Darrin J Pochan

Abstract read
In one paragraph

Article in Biomacromolecules, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Polymorphism in peptide self-assembly visualized.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Protein Based Biomaterials for Therapeutic and Diagnostic Applications.Progress in biomedical engineering (Bristol, England) · 2022
    Article
  9. Article
  10. Review
  11. Infinite Assembly of Folded Proteins in Evolution, Disease, and Engineering.Angewandte Chemie (International ed. in English) · 2019
    Review
  12. Review
  13. Enzymatic Control of the Conformational Landscape of Self-Assembling Peptides.Angewandte Chemie (International ed. in English) · 2018
    Article
  14. Multicomponent peptide assemblies.Chemical Society reviews · 2018
    Review
  15. Article
  16. Article
  17. β-hairpin peptide hydrogels for package delivery.Advanced drug delivery reviews · 2017
    Review
  18. Peptide-Based Supramolecular Hydrogels for Delivery of Biologics.Bioengineering & translational medicine · 2016
    Article
  19. Article
  20. 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

8 authors.

Sameer SathayeDepartment of Materials Science and Engineering and Delaware Biotechnology Institute, University of Delaware , Newark, Delaware 19716, United States.
Huixi Zhang
Cem Sonmez
Joel P Schneider
Christopher M MacDermaid
Christopher D Von Bargen
Jeffery G Saven
Darrin J Pochan

Funding

Design and Utility of Novel Protienaceous BiomaterialsZIABC011313 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SCHNEIDER, JOEL · 2010 to 2025
$19.0M
Fundamentals of Ligand-Protein InteractionsZIABC010832 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NICKLAUS, MARC · 2009 to 2024
$1.7M
Intramural NIH HHS ZIA BC010832
6 · The paper itself

Abstract

The MAX1 β-hairpin peptide (VKVKVKVK-V(D)PPT-KVKVKVKV-NH2) has been shown to form nanofibrils having a cross-section of two folded peptides forming a hydrophobic, valine-rich core, and the polymerized fibril exhibits primarily β-sheet hydrogen bonding.1-7 These nanofibrils form hydrogel networks through fibril entanglements as well as fibril branching.8 Fibrillar branching in MAX1 hydrogel networks provide the ability to flow under applied shear stress and immediately reform a hydrogel solid on cessation of shear. New β-hairpins were designed to limit branching during nanofibril growth because of steric specificity in the assembled fibril hydrophobic core. The nonturn valines of MAX1 were substituted by 2-naphthylalanine (Nal) and alanine (A) residues, with much larger and smaller side chain volumes, respectively, to obtain LNK1 (Nal)K(Nal)KAKAK-V(D)PPT-KAKAK(Nal)K(Nal)-NH2. LNK1 was targeted to self-associate with a specific "lock and key" complementary packing in the hydrophobic core in order to accommodate the Nal and Ala residue side chains. The experimentally observable manifestation of reduced fibrillar branching in the LNK1 peptide is the lack of solid hydrogel formation after shear in stark contrast to the MAX1 branched fibril system. Molecular dynamics simulations provide a molecular picture of interpeptide interactions within the assembly that is consistent with the branching propensity of MAX1 vs LNK1 and in agreement with experimental observations.

Indexed as

Hydrophobic and Hydrophilic InteractionsChemical EngineeringHydrogelsPeptide FragmentsProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryHydrogelsPeptide Fragments

Identifiers

PMID25251904
PMCPMC7720678

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.