Dielectric properties of Bauhinia monandra and Concanavalin A lectin monolayers, part I

Andrade, César A.S.; Baszkin, Adam; Santos-Magalhães, Nereide Stela; Coelho, Luana Cassandra Breitenbach Barroso; Melo, Celso P. de

doi:10.1016/j.jcis.2005.01.076

Cited by 12 publications

(8 citation statements)

References 39 publications

(43 reference statements)

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“…To improve the reliability of protein CD analysis, three programs (CONTIN, SELCON3 and CDSSTR) were used, which resulted in a less than 2.0% deviation. The lectin of B. monandra (Bmoll) also has ␣-helices in its structure [40], although B. purpurea and B. variegata candida lectins structures are predominantly ␤-sheet. The lectin from B. purpurea contains 65% ␤-sheet, 19% ␤-turn and no ␣-helices [16], which is very similar to that described for the lectin (BvcL) from B. variegata candida [11].…”

Section: Structural Characterizationmentioning

confidence: 99%

Purification, primary structure and potential functions of a novel lectin from Bauhinia forficata seeds

Silva

Santana

Mentele

et al. 2012

Process Biochemistry

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A new lectin, BfL, was purified from Bauhinia forficata seeds by ammonium sulfate fractionation, DEAE-Sephadex ion exchange chromatography, Sepharose-4B and chitin affinity chromatographies and Superdex 75 size exclusion chromatography. The molecular homogeneity and purity of BfL were assessed by reversed-phase HPLC. BfL appeared as a single band of approximately 27.0 kDa on SDS-PAGE under non-reducing and reducing conditions, and its molecular weight was determined to be 27,850 Da by LC/ESI-MS. BfL is a glycoprotein with a carbohydrate content of 6.24% determined by the phenol-sulfuric acid method. Fetuin, asialofetuin, thyroglobulin and azocasein inhibited the hemagglutinating activity of BfL, whereas saccharides did not. BfL hemagglutinating activity was stable at 100 • C for 30 min, pHdependent, with the highest activity at pH 6.0, and metal-independent. The primary structure of BfL shows similarity with other lectins from the genus Bauhinia. Deconvolution of the BfL circular dichroism (CD) spectrum indicated the presence of ␣-helix and ␤ structures. BfL increases coagulation time, but this effect is not related to human plasma kallikrein or human factor Xa inhibition. BfL also inhibits ADPand epinephrine-induced platelet aggregation in a dose-dependent manner and is the only currently described lectin from Bauhinia that exhibits anticoagulant and antiplatelet aggregating properties.

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Section: Structural Characterizationmentioning

confidence: 99%

Purification, primary structure and potential functions of a novel lectin from Bauhinia forficata seeds

Silva

Santana

Mentele

et al. 2012

Process Biochemistry

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“…Polyaniline (PANI) reveals redox functions only in acid media (pH < 4) [11] a feature that limits its broad use, specifically in combination with biomaterials. However, BmoLL is stable in this pH range and has a negative surface charge [12].…”

Section: Introductionmentioning

confidence: 96%

Diagnosis of dengue infection using a modified gold electrode with hybrid organic–inorganic nanocomposite and Bauhinia monandra lectin

Andrade¹,

Oliveira²,

Melo³

et al. 2011

Journal of Colloid and Interface Science

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A sensitive and selective biosensor for dengue serotyping was successfully developed. The biosensor uses a novel gold nanoparticles-polyaniline hybrid composite (AuNpPANI) for the immobilization of Bauhinia monandra lectin (BmoLL). The nanocomposite was applied to a bare gold electrode surface by chemical adsorption, and BmoLL was subsequently electrostatically adsorbed to the nanocomposite-modified surface. Atomic force microscopy (AFM), cyclic voltammetry (CV) and electrochemical impedance (EI) techniques were applied to evaluate the immobilization of BmoLL on AuNpPANI. The AFM images for AuNpPANI-BmoLL-DEN systems indicate a homogenous, compact and dense film of the conjugate. In the EI analyses, an obvious difference of the electron transfer resistance between the AuNpPANI-modified electrode and the bare gold electrode was observed. Among three dengue serotypes studied, dengue serotype 2 (DEN2) has higher values for R(CT), and lower values for both n and Q. These are indications of a larger blocking effect and smaller capacitive dispersion, resulting from the higher agglutination of glycoproteins from the DEN2 sera. The selective BmoLL recognition for various dengue serotypes may be attributed to different patterns of glycoproteins in the sera produced by the glycoprotein immunoresponse from patients infected by the dengue virus.

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“…All these protein monolayers were found to be stable and to have preserved their native conformation after spreading. Recently, monolayers of the antibiotic peptides maculatin and citropin [31] and of Bauhinia monandra (Bmoll) and concanavalin A (Con A) lectins [32] were shown to be stable under lateral compression.…”

Section: Proteins At Interfacesmentioning

confidence: 99%

Dielectric properties of Bauhinia monandra and Concanavalin A lectin monolayers, part I

Cited by 12 publications

References 39 publications

Purification, primary structure and potential functions of a novel lectin from Bauhinia forficata seeds

Purification, primary structure and potential functions of a novel lectin from Bauhinia forficata seeds

Diagnosis of dengue infection using a modified gold electrode with hybrid organic–inorganic nanocomposite and Bauhinia monandra lectin

Molecular recognition on the supported and on the air/water interface-spread protein monolayers

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