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Titolo:
Scanning electron microscopy studies of protein-functionalized atomic force microscopy cantilever tips
Autore:
Micic, M; Chen, A; Leblanc, RM; Moy, VT;
Indirizzi:
Univ Miami, Sch Med, Dept Physiol & Biophys, Miami, FL 33136 USA Univ Miami Miami FL USA 33136 Dept Physiol & Biophys, Miami, FL 33136 USA Univ Miami, Dept Chem, Ctr Supramol Sci, Miami, FL 33152 USA Univ Miami Miami FL USA 33152 Chem, Ctr Supramol Sci, Miami, FL 33152 USA Univ Miami, Program Neurosci, Miami, FL 33152 USA Univ Miami Miami FL USA33152 iami, Program Neurosci, Miami, FL 33152 USA
Titolo Testata:
SCANNING
fascicolo: 6, volume: 21, anno: 1999,
pagine: 394 - 397
SICI:
0161-0457(199911/12)21:6<394:SEMSOP>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Keywords:
atomic force microscopy; scanning electron microscopy; protein adsorption; ligand-receptor interactions;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
12
Recensione:
Indirizzi per estratti:
Indirizzo: Moy, VT Univ Miami, Sch Med, Dept Physiol & Biophys, 1600 NW 10th Ave, Miami, FL 33136 USA Univ Miami 1600 NW 10th Ave Miami FL USA 33136 Miami, FL 33136 USA
Citazione:
M. Micic et al., "Scanning electron microscopy studies of protein-functionalized atomic force microscopy cantilever tips", SCANNING, 21(6), 1999, pp. 394-397

Abstract

Protein-functionalized atomic force microscopy (AFM) tips have been used to investigate the interaction of individual ligand-receptor complexes. Herein we present results from scanning electron microscopy (SEM) studies of protein-functionalized AFM cantilever tips. The goals of this study were (1) to examine the surface morphology of protein-coated AFM tips and (2) to determine the stability of the coated tips. Based on SEM images. we found thatbovine serum albumin (BSA) in solution spontaneously adsorbed onto the surface of silicon nitride cantilevers, forming a uniform protein layer over the surface. Additional protein layers deposited over the initial BSA-coatedsurface did not significantly alter the surface morphology. However, we found that avidin-functionalized rips were contaminated with debris after a series of force measurements with biotinylated agarose beads. The bound debris presumably originated from the transfer of material from the agarose bead. This observation is consistent with the observed deterioration of functional activity as measured in ligand-receptor binding force experiments.

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Documento generato il 02/07/20 alle ore 22:08:41