Evidence map›Paper›PMID 36926896›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2023

Highly Hydrophobic Films of Engineered Silk Proteins by a Simple Deposition Method.

Teemu Välisalmi, Nelmary Roas-Escalona, Kristoffer Meinander, Pezhman Mohammadi, Markus B Linder

Open access · hybridAbstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.1field-weighted citation impact, top 27% 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

3 citing papers in PubMed, 11 citations in OpenAlex.

  1. Biosynthetic optical waveguide interface integration using biomimetic -Computational and structural biotechnology journal · 2026
    Article
  2. Pollen-inspired biopolymer-based multifunctional films.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. 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

5 authors at 2 institutions in 1 country.

Teemu VälisalmiDepartment of Bioproducts and Biosystems, School of Chemical Engineering, Aalto University, FI-00076 Aalto, Finland.ORCID 0000-0001-9704-5560
Nelmary Roas-EscalonaDepartment of Bioproducts and Biosystems, School of Chemical Engineering, Aalto University, FI-00076 Aalto, Finland.ORCID 0000-0002-6406-9053
Kristoffer MeinanderDepartment of Bioproducts and Biosystems, School of Chemical Engineering, Aalto University, FI-00076 Aalto, Finland.
Pezhman MohammadiVTT Technical Research Centre of Finland, Limited (VTT), FI-02044 Espoo, Finland.ORCID 0000-0003-4593-5371
Markus B LinderDepartment of Bioproducts and Biosystems, School of Chemical Engineering, Aalto University, FI-00076 Aalto, Finland.ORCID 0000-0002-7271-6441
Aalto University · FIVTT Technical Research Centre of Finland · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Molecular engineering of protein structures offers a uniquely versatile route for novel functionalities in materials. Here, we describe a method to form highly hydrophobic thin films using genetically engineered spider silk proteins. We used structurally engineered protein variants containing ADF3 and AQ12 spider silk sequences. Wetting properties were studied using static and dynamic contact angle measurements. Solution conditions and the surrounding humidity during film preparation were key parameters to obtain high hydrophobicity, as shown by contact angles in excess of 120°. Although the surface layer was highly hydrophobic, its structure was disrupted by the added water droplets. Crystal-like structures were found at the spots where water droplets had been placed. To understand the mechanism of film formation, different variants of the proteins, the topography of the films, and secondary structures of the protein components were studied. The high contact angle in the films demonstrates that the conformations that silk proteins take in the protein layer very efficiently expose their hydrophobic segments. This work reveals a highly amphiphilic nature of silk proteins and contributes to an understanding of their assembly mechanisms. It will also help in designing diverse technical uses for recombinant silk.

Indexed as

SilkSpidersAnimalsHydrophobic and Hydrophilic InteractionsRecombinant ProteinsWaterWettabilityRecombinant ProteinsSilkWater

Identifiers

PMID36926896
PMCPMC10061925
OpenAlexW4327546793

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.