Quartz crystal microbalance biosensor for recombinant human interferon-β detection based on antisense peptide approach

Luo, Jia; Zhang, Qundan; Liu, Guoquan; Zhao, Rui

doi:10.1016/j.aca.2007.03.022

Cited by 16 publications

(13 citation statements)

References 24 publications

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“…As the interactions between sense and antisense peptides are concerned, both the nature of the genetic codes and the hydropathic analysis of sense and antisense peptides suggest hydrophobic amino acids are partnered with hydrophilic ones and vice versa (Heal et al, 2002). The successful applications of this principle for designing sequence-directed recognition peptides indicate that hydropathical complementarity plays an important role in peptide interactions (Fassina et al, 1992(Fassina et al, , 1995Luo et al, 2007). In this study, the screened peptide KKKKYRNIRRPG is a positive correlation of this idea.…”

Section: Discussion On the Interaction Mechanismsmentioning

confidence: 67%

“…Evidence has accumulated to suggest antisense peptides interact specifically with their sense peptide counterparts with significant biological consequences (Heal et al, 2002). Antisense peptides have been successfully applied in the development of anti-idiotypic antibodies (Bost and Blalock, 1989;Araga et al, 1993), identification of novel receptors (Ruiz-Opazo et al, 1995), design of inhibitors of protein effectors (Davids et al, 1997;Imai et al, 2007), as well as purification or detection of proteins (Fassina et al, 2007;Luo et al 2007). However, the mechanism of interactions between sense and antisense peptides is still a matter of controversy.…”

Section: Introductionmentioning

confidence: 99%

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Design, synthesis and screening of antisense peptide based combinatorial peptide libraries towards an aromatic region of SARS‐CoV

Zhao

Luo

Xiong

et al. 2008

J of Molecular Recognition

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A combination of high-performance affinity chromatography and antisense peptide based combinatorial peptide libraries was used to screen a potential inhibitor for SARS-CoV. An aromatic-amino acid-rich region within the transmembrane domain at the C terminal of spike (S) protein identified as a membrane-active region was chosen as the target sense peptide (SP) and immobilized as affinity ligand. Four antisense peptides were designed based on the degeneracy of genetic codes. One of them was screened as the lead peptide to construct the extended peptide libraries (EPL). The library screening was carried out at pH 5.5 so as to mimic the low-pH milieu required by virus fusion. After five cycles of screening, a dodecapeptide KKKKYRNIRRPG (DP) was identified to possess the highest binding affinity to the immobilized sense peptide. The dissociation constant of the complex between the DP and the SP was 5.64 x 10(-7) M in a physiological condition. The recognition between the DP and recombinant SARS S protein was demonstrated by ELISA assay to be in a saturable way. The competitive inhibition of the sense peptide in the competitive ELISA reveals the affinity binding between the DP and SARS S protein is specific and directed towards the target SP of the S protein. The results indicate this preferred polypeptide can be used as a lead compound of potent inhibitor of SARS-CoV. The mechanism study suggests the specific recognition between the DP and the target peptide was due to sequence-dependent and multi-modal affinity interaction.

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Section: Discussion On the Interaction Mechanismsmentioning

confidence: 67%

Section: Introductionmentioning

confidence: 99%

Design, synthesis and screening of antisense peptide based combinatorial peptide libraries towards an aromatic region of SARS‐CoV

Zhao

Luo

Xiong

et al. 2008

J of Molecular Recognition

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“…Complementary peptides could be useful for drug discovery and therefore represent a conceptually attractive approach. There are some examples reported in the literature, 14,45 which suggest that interactions between sense and antisense peptides could play an important role in the molecular interactions involved in the recognition between proteins. In addition to H-bonds, peptides provide various non-covalent interactions, which are strongly dependent on the peptide sequence; thus, the recognition is specific and selective.…”

Section: Discussionmentioning

confidence: 99%

“…The successful applications of this principle for designing sequence-directed recognition peptides indicate that hydropathical complementarity plays an important role in peptide interactions. 14,45 We employed the degeneracy of the antisense peptide approach to design complementary peptides to one of the surface exposed loops of porin P2 from Haemophilus influenzae. We showed that a biologically active peptide can be obtained from a small loop structure.…”

Section: Discussionmentioning

confidence: 99%

“…5 There have been numerous reports of the successful identification of peptide-peptide interactions based on these principles. [6][7][8][9][10][11][12][13][14] However, the mechanism of interactions is still debated under two main hypotheses. In the molecular recognition theory (MRT), the sense and complementary strands of DNA must always code for peptide sequences that are opposite in hydropathic profile to each other, and therefore have mutually complementary shapes, so they should be able to interact specifically.…”

Section: Introductionmentioning

confidence: 99%

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Peptides complementary to the active loop of porin P2 from Haemophilus influenzae modulate its activity

Cantisani

Vitiello²,

Falanga³

et al. 2012

IJN

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Abstract:Haemophilus influenzae type b (Hib) is one of the leading causes of invasive bacterial infection in young children. It is characterized by inflammation that is mainly mediated by cytokines and chemokines. One of the most abundant components of the Hib outer membrane is the P2 porin, which has been shown to induce the release of several inflammatory cytokines. A synthetic peptide corresponding to loop L7 of the porin activates JNK and p38 mitogenactivated protein kinase (MAPK) pathways. We report a novel use of the complementary peptide approach to design a peptide that is able to bind selectively to the protein P2, thereby reducing its activity. This work provides insights into essential molecular details of P2 that may affect the pathogenesis of Hib infections where interruption of the signaling cascade could represent an attractive therapeutic strategy.

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A survey of the 2006–2009 quartz crystal microbalance biosensor literature

Becker

Cooper

2011

J of Molecular Recognition

161

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Since the publication of the original review of piezoelectric acoustic sensors in this series there has been a consistent, gradual expansion in the number of published papers using 'quartz crystal microbalances' (QCM). Between 2001 and 2009, the number of QCM publications per annum has increased from 49 to 273, with a two-fold increase in papers per annum between 2004 and 2008. Within the field, comparing the time covered by the current to the previous review, there are trends towards increasing use of QCM in the study of protein adsorption to surfaces (93% increase), homeostasis (67% increase), protein-protein interactions (40% increase) and carbohydrates (43% increase). New commercial systems have been released that are driving the uptake of the technology for characterization of binding specificities, affinities, kinetics and conformational changes associated with a molecular recognition event. This paper highlights theoretical and practical aspects of the principles 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 membrane interfaces.

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Quartz crystal microbalance biosensor for recombinant human interferon-β detection based on antisense peptide approach

Cited by 16 publications

References 24 publications

Design, synthesis and screening of antisense peptide based combinatorial peptide libraries towards an aromatic region of SARS‐CoV

Design, synthesis and screening of antisense peptide based combinatorial peptide libraries towards an aromatic region of SARS‐CoV

Peptides complementary to the active loop of porin P2 from Haemophilus influenzae modulate its activity

A survey of the 2006–2009 quartz crystal microbalance biosensor literature

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