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Peptides for functionalization of InP semiconductors
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2009 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 337, no 2, 358-363 p.Article in journal (Refereed) Published
Abstract [en]

The challenge is to achieve high specificity in molecular sensing by proper functionalization of micro/nano-structured semiconductors by peptides that reveal specific recognition for these structures. Here we report on surface modification of the InP semiconductors by adhesion peptides produced by the phage display technique. An M13 bacteriophage library has been used to screen 10(10) different peptides against the InP(0 0 1) and the InP(1 1 1) surfaces to finally isolate specific peptides for each orientation of the InP. MALDI-TOF/TOF mass spectrometry has been employed to study real affinity of the peptide towards the InP surfaces. The peptides serve for controlled placement of biotin onto InP to bind then streptavidin. Our Atomic Force Microscopy study revealed a total surface coverage of molecules when the InP surface was functionalized by its specific biotinylated peptide (YAIKGPSHFRPS). Finally, fluorescence microscopy has been employed to demonstrate the preferential attachment of the peptide onto a micro-patterned InP surface. Use of substrate specific peptides could present an alternative solution for the problems encountered in the actually existing sensing methods and molecular self-assembly due to the unwanted unspecific interactions.

Place, publisher, year, edition, pages
2009. Vol. 337, no 2, 358-363 p.
Keyword [en]
Functionalization, Bacteriophage, Specific peptide, Semiconductors, Mass spectroscopy, quantum dots, phage display, protein, nanocrystals, luminescent, recognition, surfaces
Identifiers
URN: urn:nbn:se:kth:diva-18667DOI: 10.1016/j.jcis.2009.05.040ISI: 000268740500007Scopus ID: 2-s2.0-67650985973OAI: oai:DiVA.org:kth-18667DiVA: diva2:336714
Note
QC 20100525Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2017-12-12Bibliographically approved

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Lourdudoss, Sebastian

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CiteExportLink to record
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  • apa
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  • de-DE
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