Evidence map›Paper›PMID 31891067›Full record

ArticleACS omega2019

Serum Albumin-Peptide Conjugates for Simultaneous Heparin Binding and Detection.

Qing Liu, Salla Välimäki, Ahmed Shaukat, Boxuan Shen, Veikko Linko, Mauri A Kostiainen

Open access · goldAbstract read
In one paragraph

Article in ACS omega, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

  1. Engineering Host-Guest Interactions for Next-Generation Heparin Biosensors.Small (Weinheim an der Bergstrasse, Germany) · 2026
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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 1 institution in 1 country.

Qing LiuBiohybrid Materials, Department of Bioproducts and Biosystems and HYBER Center of Excellence, Department of Applied Physics, Aalto University, 00076 Aalto, Finland.
Salla VälimäkiBiohybrid Materials, Department of Bioproducts and Biosystems and HYBER Center of Excellence, Department of Applied Physics, Aalto University, 00076 Aalto, Finland.
Ahmed ShaukatBiohybrid Materials, Department of Bioproducts and Biosystems and HYBER Center of Excellence, Department of Applied Physics, Aalto University, 00076 Aalto, Finland.
Boxuan ShenBiohybrid Materials, Department of Bioproducts and Biosystems and HYBER Center of Excellence, Department of Applied Physics, Aalto University, 00076 Aalto, Finland.
Veikko LinkoBiohybrid Materials, Department of Bioproducts and Biosystems and HYBER Center of Excellence, Department of Applied Physics, Aalto University, 00076 Aalto, Finland.
Mauri A KostiainenBiohybrid Materials, Department of Bioproducts and Biosystems and HYBER Center of Excellence, Department of Applied Physics, Aalto University, 00076 Aalto, Finland.
Aalto University · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heparin is a polysaccharide-based anticoagulant agent, which is widely used in surgery and blood transfusion. However, overdosage of heparin may cause severe side effects such as bleeding and low blood platelet count. Currently, there is only one clinically licensed antidote for heparin: protamine sulfate, which is known to provoke adverse effects. In this work, we present a stable and biocompatible alternative for protamine sulfate that is based on serum albumin, which is conjugated with a variable number of heparin-binding peptides. The heparin-binding efficiency of the conjugates was evaluated with methylene blue displacement assay, dynamic light scattering, and anti-Xa assay. We found that multivalency of the peptides played a key role in the observed heparin-binding affinity and complex formation. The conjugates had low cytotoxicity and low hemolytic activity, indicating excellent biocompatibility. Furthermore, a sensitive DNA competition assay for heparin detection was developed. The detection limit of heparin was 0.1 IU/mL, which is well below its therapeutic range (0.2-0.4 IU/mL). Such biomolecule-based systems are urgently needed for next-generation biocompatible materials capable of simultaneous heparin binding and sensing.

Identifiers

PMID31891067
PMCPMC6933801
OpenAlexW2995360513

What OpenQuestion holds

Textmetadata
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.