Object's details: Comparison of α-Helix and β-Sheet Structure Adaptation to a Quantum Dot Geometry: Toward the Identification of an Optimal Motif for a Protein Nanoparticle Cover

Provider:Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

Description

Title:
Comparison of α-Helix and β-Sheet Structure Adaptation to a Quantum Dot Geometry: Toward the Identification of an Optimal Motif for a Protein Nanoparticle Cover
Creator:
Kopeć, Katarzyna;
Pędziwiatr, Marta;
Gront, Dominik;
Sztatelman, Olga;
Sławski, Jakub;
Łazicka, Magdalena;
Worch, Remigiusz;
Zawada, Katarzyna;
Makarova, Katerina;
Nyk, Marcin;
Grzyb, Joanna
Description:
While quantum dots (QDs) are useful as fluorescent labels, their application in biosciences is limited due to the stability and hydrophobicity of their surface. In this study, we tested two types of proteins for use as a cover for spherical QDs, composed of cadmium selenide. Pumilio homology domain (Puf), which is mostly α-helical, and leucine-rich repeat (LRR) domain, which is rich in β-sheets, were selected to determine if there is a preference for one of these secondary structure types for nanoparticle covers. The protein sequences were optimized to improve their interaction with the surface of QDs. The solubilization of the apoproteins and their assembly with nanoparticles required the application of a detergent, which was removed in subsequent steps. Finally, only the Puf-based cover was successful enough as a QD hydrophilic cover. We showed that a single polypeptide dimer of Puf, PufPuf, can form a cover. We characterized the size and fluorescent properties of the obtained QD:protein assemblies. We showed that the secondary structure of the Puf proteins was not destroyed upon contact with the QDs. We demonstrated that these assemblies do not promote the formation of reactive oxygen species during illumination of the nanoparticles. The data represent advances in the effort to obtain a stable biocompatible cover for QDs.
Object availability:
free access
Date:
2019.08.05
Type:
Article;
PeerReviewed
Language:
English
Format:
application/pdf
Publisher:
ACS Publications
Relation: http://eprints.ibb.waw.pl/1745 ;https://pubs.acs.org/journal/acsodf ;doi.org/10.1021/acsomega.9b00505
Subject:
QD Chemistry;
QH301 Biology
Identifier: http://eprints.ibb.waw.pl/1745/1/acsomega.9b00505.pdf ;
Kopeć, Katarzyna and Pędziwiatr, Marta and Gront, Dominik and Sztatelman, Olga and Sławski, Jakub and Łazicka, Magdalena and Worch, Remigiusz and Zawada, Katarzyna and Makarova, Katerina and Nyk, Marcin and Grzyb, Joanna (2019) Comparison of α-Helix and β-Sheet Structure Adaptation to a Quantum Dot Geometry: Toward the Identification of an Optimal Motif for a Protein Nanoparticle Cover. ACS Omega, 4 (8). pp. 13086-13099. ISSN 2470-1343
Data provider:
Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

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Object's details: Comparison of α-Helix and β-Sheet Structure Adaptation to a Quantum Dot Geometry: Toward the Identification of an Optimal Motif for a Protein Nanoparticle Cover

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