Immobilization of sunflower trypsin inhibitor (SFTI-1) peptide onto a gold surface and analysis of its interaction with trypsin

Ohtsuka, Keiichi; Kajiki, Ryo; Waki, Michinori; Nojima, Takahiko; Takenaka, Shigeori

doi:10.1039/b409178g

Cited by 9 publications

(7 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The quartz crystal microbalance-dissipation (QCM-D) technique has been shown to be highly sensitive to the mass changes and to the viscoelastic properties of an adlayer. − It has been widely utilized in nanorange mass detection due to its high sensitivity, reliability, and simplicity. It is also a popular instrument for in situ measurements of biomacromolecular interactions in liquid-state research applications. − Finally, it has been proven to be a valuable technique for studying interactions between biomacromolecules at liquid−solid interfaces including protein−lipid bilayer, − cell−cell , and antibody−antigen interactions, − as well as biological signal transduction processes , and biomolecule detection. − …”

mentioning

confidence: 99%

Alpha-Helical Peptide-Induced Vesicle Rupture Revealing New Insight into the Vesicle Fusion Process As Monitored in Situ by Quartz Crystal Microbalance-Dissipation and Reflectometry

et al. 2009

View full text Add to dashboard Cite

We have used simultaneous quartz crystal microbalance-dissipation (QCM-D) monitoring and four-detector optical reflectometry to monitor in situ the structural transformation of intact vesicles to a lipid bilayer on a gold surface. The structural transformation of lipid vesicles to a bilayer was achieved by introducing a particular amphipathic, alpha-helical (AH) peptide. The combined experimental apparatus allows us to simultaneously follow the acoustic and optical property changes of the vesicle rupturing process upon interaction with AH peptides. While QCM-D and reflectometry have similar sensitivities in terms of mass and thickness resolution, there are unique advantages in operating these techniques simultaneously on the same substrate. These advantages permit us to (1) follow the complex interaction between AH peptides and intact vesicles with both acoustic and optical mass measurements, (2) calculate the amount of dynamically coupled water during the interaction between AH peptides and intact vesicles, (3) demonstrate that the unexpectedly large increase of both adsorbed mass and the film's energy dissipation is mainly caused by swelling of the vesicles during the binding interaction with AH peptides, and (4) permit us to understand the structural transformation from intact vesicles to a bilayer via the AH peptide interaction by monitoring viscoelastic properties, acoustic mass, optical mass, and thickness changes of both the binding and destabilization processes. From the deduced "hydration signature" we followed the complex transformation of lipid assemblies. On the basis of this information, a mechanism of this structural transformation is proposed that provides new insight into the process of vesicle fusion on solid substrates.

show abstract

mentioning

confidence: 99%

Alpha-Helical Peptide-Induced Vesicle Rupture Revealing New Insight into the Vesicle Fusion Process As Monitored in Situ by Quartz Crystal Microbalance-Dissipation and Reflectometry

et al. 2009

View full text Add to dashboard Cite

show abstract

“…QCM was also used to investigate the influence of cations, anions and solvent on protein-protein interactions (Sadik and Cheung, 2001). Other examples of QCM in the study of peptide-peptide and peptide-proteins interactions include (Samoylov et al, 2002;Laricchia-Robbio and Revoltella, 2004;Miura et al, 2004;Ohtsuka et al, 2004;Lung et al, 2005;Takakusagi et al, 2005;Shen et al, 2005a).…”

Section: Protein-proteinmentioning

confidence: 99%

A survey of the 2001 to 2005 quartz crystal microbalance biosensor literature: applications of acoustic physics to the analysis of biomolecular interactions

Cooper¹,

Singleton²

2007

J of Molecular Recognition

336

205

View full text Add to dashboard Cite

The widespread exploitation of biosensors in the analysis of molecular recognition has its origins in the mid-1990s following the release of commercial systems based on surface plasmon resonance (SPR). More recently, platforms based on piezoelectric acoustic sensors (principally 'bulk acoustic wave' (BAW), 'thickness shear mode' (TSM) sensors or 'quartz crystal microbalances' (QCM)), have been released that are driving the publication of a large number of papers analysing binding specificities, affinities, kinetics and conformational changes associated with a molecular recognition event. This article highlights salient theoretical and practical aspects of the technologies that underpin acoustic analysis, then reviews exemplary papers in key application areas involving small molecular weight ligands, carbohydrates, proteins, nucleic acids, viruses, bacteria, cells and lipidic and polymeric interfaces. Key differentiators between optical and acoustic sensing modalities are also reviewed.

show abstract

“…Firstly, the RNase S-peptide (1-19) 16 was assembled on the Model 433A peptide synthesizer on a 0.25 mmol scale using Fmoc-Ala-Alko-resin (0.7 mmol g 21 , Watanabe Chemical Industries, Ltd., Japan) and the FastMoc protocol as described previously. 17 Fmoc-8amino-3,6-dioxaoctanoic acid (Peptide International Inc., USA) as a linker chain was coupled twice to the N-terminus of the peptide-resin. The peptide-resin (167 mg, 35.6 mmol) removed from the reaction vessel was suspended in 1.5 mL of N-methylpyrrolidone (NMP) and stirred for 30 min at room temperature to be swelled.…”

Section: Preparation Of Oligonucleotide-peptide Conjugatementioning

confidence: 99%

“…A 27 MHz, AT-cut QCM sensor chip (Initium Co., Japan) 17,21,22 covered with a gold surface (diameter: 2.5 mm; area: 4.9 mm 2 ) was used in the QCM experiment. CapOligo, 59-thiolated oligonucleotide (59-HS-(CH 2 ) 6 -ACT GGC CGT CGT TTT ACA ACG TCG) custom-synthesized by Genenet Co., Japan, could be immobilized on the gold surface of the QCM chip with good reproducibility in the following procedure (Fig.…”

Section: Preparation Of Ssdna-fixed Qcm Chipmentioning

confidence: 99%

“…Competitive experiment was performed in the presence of S-peptide analogs, LB2, 16 A5W, 16 S-peptide or sunflower trypsin inhibitor (SFTI-1). 17 The S-peptide analogs, LB2 and A5W, have been shown to bind to S-protein with high affinity by the surface plasmon resonance experiment and their enzymatic activities. 16 SFTI-1 was used as a negative control with a nonbinding property to S-protein.…”

Section: Evaluation Of Specific Interaction Of S-protein With S-pepti...mentioning

confidence: 99%

See 1 more Smart Citation

Immobilization of RNase S-Peptide on a single-stranded DNA-fixed gold surface and effective masking of its surface by an acridinyl poly(ethylene glycol)

Ohtsuka

Uemura

Nojima

et al. 2006

Analyst

Self Cite

View full text Add to dashboard Cite

Oligonucleotide-peptide conjugate was synthesized by coupling of RNase S-peptide to a 24-mer single-stranded DNA (ssDNA) oligonucleotide to be immobilized on its complementary ssDNA oligonucleotide-fixed gold surface of sensor chip or electrode. Immobilization of on the ssDNA-fixed gold surface through DNA duplex formation was confirmed by quartz crystal microbalance (QCM) and electrochemical measurements. After treating with a synthetic acridinyl poly(ethylene glycol) (APEG), specific interaction of S-protein with the S-peptide immobilized on the gold surface was demonstrated by QCM without nonspecific adsorption of unrelated proteins such as BSA and RNase A at the surfaces. This result suggested that the acridine parts of APEG could bind to the DNA duplex on the gold surface and the poly(ethylene glycol) parts were fastened on the surface to resist the adsorption of proteins. Thus, the combination of oligonucleotide-peptide conjugate, ssDNA-fixed chip and APEG with effective masking property provides a new tool for the analysis of specific peptide-protein interactions without disturbance by other unrelated proteins.

show abstract

Immobilization of sunflower trypsin inhibitor (SFTI-1) peptide onto a gold surface and analysis of its interaction with trypsin

Abstract: Sunflower trypsin inhibitor (SFTI-1) derived peptide having one disulfide bond could be immobilized via a thiol-disulfide exchange reaction onto a gold surface on a quartz crystal microbalance (QCM) chip. This permitted quantitative analysis of the specific interaction with trypsin.

Cited by 9 publications

References 19 publications

Alpha-Helical Peptide-Induced Vesicle Rupture Revealing New Insight into the Vesicle Fusion Process As Monitored in Situ by Quartz Crystal Microbalance-Dissipation and Reflectometry

Alpha-Helical Peptide-Induced Vesicle Rupture Revealing New Insight into the Vesicle Fusion Process As Monitored in Situ by Quartz Crystal Microbalance-Dissipation and Reflectometry

A survey of the 2001 to 2005 quartz crystal microbalance biosensor literature: applications of acoustic physics to the analysis of biomolecular interactions

Immobilization of RNase S-Peptide on a single-stranded DNA-fixed gold surface and effective masking of its surface by an acridinyl poly(ethylene glycol)

Contact Info

Product

Resources

About