Serum Albumin-Peptide Conjugates for Simultaneous Heparin Binding and Detection

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Serum Albumin-Peptide Conjugates for Simultaneous Heparin Binding and Detection. / Liu, Qing; Välimäki, Salla; Shaukat, Ahmed; Shen, Boxuan; Linko, Veikko; Kostiainen, Mauri A.

julkaisussa: ACS Omega, 2019, s. 21891-21899.

Tutkimustuotos: Lehtiartikkelivertaisarvioitu

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@article{dec3283c9e724c5ea86fd20d00c73071,
title = "Serum Albumin-Peptide Conjugates for Simultaneous Heparin Binding and Detection",
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.",
author = "Qing Liu and Salla V{\"a}lim{\"a}ki and Ahmed Shaukat and Boxuan Shen and Veikko Linko and Kostiainen, {Mauri A.}",
year = "2019",
doi = "10.1021/acsomega.9b02883",
language = "English",
pages = "21891--21899",
journal = "ACS Omega",
issn = "2470-1343",
publisher = "AMERICAN CHEMICAL SOCIETY",

}

RIS - Lataa

TY - JOUR

T1 - Serum Albumin-Peptide Conjugates for Simultaneous Heparin Binding and Detection

AU - Liu, Qing

AU - Välimäki, Salla

AU - Shaukat, Ahmed

AU - Shen, Boxuan

AU - Linko, Veikko

AU - Kostiainen, Mauri A.

PY - 2019

Y1 - 2019

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85076768735&partnerID=8YFLogxK

U2 - 10.1021/acsomega.9b02883

DO - 10.1021/acsomega.9b02883

M3 - Article

AN - SCOPUS:85076768735

SP - 21891

EP - 21899

JO - ACS Omega

JF - ACS Omega

SN - 2470-1343

ER -

ID: 40315211