Force spectroscopic detection of peptide cleavage by thrombin exploiting biotin–streptavidin interactions in a bio-sensing context-Reference-Cited by-同舟云学术

Force spectroscopic detection of peptide cleavage by thrombin exploiting biotin–streptavidin interactions in a bio-sensing context

Published:2019 Issue:8 Volume:11 Page:1102-1110
ISSN:1759-9660
Container-title:Analytical Methods
language:en
Short-container-title:Anal. Methods

Author:

Li Jingfeng¹²³⁴⁵^ORCID,Li Qing¹²³⁴⁵,Potthoff Sebastian¹²³⁴⁵^ORCID,Wei Gang¹²³⁴⁵^ORCID,Lucio Colombi Ciacchi¹²³⁴⁵^ORCID

Affiliation:

1. University of Bremen

2. Hybrid Materials Interfaces Group

3. Faculty of Production Engineering

4. Center for Environmental Research and Sustainable Technology (UFT)

5. MAPEX Center for Materials and Processes

Abstract

Atomic-force-microscopy-based single-molecule force spectroscopy (AFM-SMFS) has become an important technique as the basis of novel, label-free biosensing strategies.

Funder

Deutsche Forschungsgemeinschaft

China Scholarship Council

Publisher

Royal Society of Chemistry (RSC)

Subject

General Engineering,General Chemical Engineering,Analytical Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2019/AY/C8AY02519C

Reference55 articles.

1. Adhesive properties of osteopontin: regulation by a naturally occurring thrombin-cleavage in close proximity to the GRGDS cell-binding domain.

2. Interaction of peptides with graphene oxide and its application for real-time monitoring of protease activity

3. Intermolecular Forces and Energies Between Ligands and Receptors

4. In situ observation of streptavidin-biotin binding on an immunoassay well surface using an atomic force microscope

5. Energy landscapes of receptor–ligand bonds explored with dynamic force spectroscopy

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