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Protein-Ligand Interactions: A Biophysical Approach

Bishnu P ChatterjeeShuvendu SnighaGautam MondalUrmimala ChatterjeePartha P BoseTapan K Ganguly

Department of Natural Sciences, West Bengal University of TechnologyDivision of Molecular Medicine, Bose InstituteSchool of Laser and Engineering, Jadavpur University

摘要:Interactions of two sialic acid binding lectins viz., Saracin, a lectin isolated from the seed integument of Saraca indica(Ashok) tree and another Sambucus nigra agglutinin(SNA) with N-acetyl neuramininc acid(NANA) have been studied by using UV–vis absorption, steady state and time resolved fluorescence along with circular dichroism(CD) spectroscopy. This study revealed that SNA–NANA system formed relatively stronger ground state complex than saracin–NANA pair. Further CD measurements substantiated the propositions made from steady state and time resolved spectroscopic investigations. It was inferred that during interaction of SNA with NANA, the lectin adopted a relatively looser conformation with the extended polypeptide structures leading to the exposure of the hydrophobic cavities which favoured stronger binding with NANA. Among the two lectins SNA forms stronger binding complex in the ground state with gold nanoparticles(GNPs) relative to saracin. Synchronous fluorescence spectral measurements further substantiate this proposition of exhibiting the fully exposed tryptophan residue in case of SNA. It appears that the lectin SNA adopted a relatively looser conformation with the extended polypeptide structures leading to the exposure of the hydrophobic cavities which favoured stronger binding with GNPs. CD measurements demonstrate that interaction of gold nanoparticles with the lectin showed no significant distortion in the structural pattern of the later. The unaltered in the secondary structural pattern of both SNA and saracin in presence of gold nanoparticles hints that GNPs may be used as useful drug or drug delivery systems. By SPR analysis the reactivity of OAW-42 ovarian cancer cell secreted alpha-1 acid glycoprotein(AGP) was monitored with three different lectins viz., Aleuria aurantia lectin(AAL), Sambucus nigra agglutinin(SNA) and Phaseolus vulgaris erythroagglutinin(E-PHA) respectively that showed more reactivity with E-PHA than other two lectin
会议名称:

第九届亚洲生物物理大会

会议时间:

2015-05-09

会议地点:

中国浙江杭州

  • 专辑:

    基础科学

  • 专题:

    生物学

  • 分类号:

    Q61

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