NDLI: Identification of materials' binding peptide sequences guided by a MALDI-ToF MS depletion assay

Content Provider	Royal Society of Chemistry (RSC)
Author	Schneider, Julian Ciacchi, Lucio Colombi Rischka, Klaus Grunwald, Ingo Steckbeck, Sascha Wittig, Linda
Copyright Year	2014
Abstract	We introduce a novel technique for an initial identification of peptide sequences that specifically bind to material surfaces based on the matrix assisted laser desorption ionization time of flight mass spectrometry (MALDI-ToF MS) depletion method. The technique relies upon time-resolved, sensitive measurements of the MALDI-ToF MS peak signals acquired from a solution containing several peptides placed in contact with an inorganic surface, in our case amorphous SiO2. Large errors intrinsic in the MALDI-ToF MS spectral analysis and uncertainties arising from the adsorption behaviour of peptide mixtures limit the predictive power of the method. However, when combined with other characterisation and modelling techniques, such as High-Performance Liquid Chromatography (HPLC), Atomic Force Microscopy (AFM), Quartz Crystal Microbalance with Dissipation (QCM-D) and Molecular Dynamics (MD), it can be used as a guide to identify novel material-binding peptide sequences, such as TPGSR for SiO2. The strategy presented in this work may have an impact on the design and synthesis of novel hybrid biomaterials based on the biomolecular recognition of inorganic surfaces.
Starting Page	1501
Ending Page	1509
Page Count	9
File Format	HTM / HTML PDF
ISSN	17599660
Volume Number	6
Issue Number	5
Journal	Analytical Methods
DOI	10.1039/c3ay42042f
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	Molecular Dynamics Molecular dynamics Atomic Force Microscopy High-performance liquid chromatography Composite material Chromatography Quartz crystal microbalance with dissipation monitoring Adsorption Atomic-force microscopy Ionization Laser Quartz Crystal Microbalance Biomaterial The Technique Peptide Mass spectrometry
Content Type	Text
Resource Type	Article
Subject	Analytical Chemistry Engineering Chemical Engineering

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