Complex Formation of Amphotericin B in Sterol-Containing Membranes As Evidenced by Surface Plasmon Resonance†

Biochemistry ◽  
2008 ◽  
Vol 47 (30) ◽  
pp. 7807-7815 ◽  
Author(s):  
Ryota Mouri ◽  
Keiichi Konoki ◽  
Nobuaki Matsumori ◽  
Tohru Oishi ◽  
Michio Murata
Keyword(s):  
Surface Plasmon Resonance ◽  
Complex Formation ◽  
Amphotericin B ◽  
Surface Plasmon ◽  
Plasmon Resonance

Thermodynamic and kinetic study of epigallocatechin-3-gallate-bovine lactoferrin complex formation determined by surface plasmon resonance (SPR): A comparative study with fluorescence spectroscopy

2019 ◽  
Vol 95 ◽  
pp. 526-532 ◽  
Author(s):  
Jaqueline de Paula Rezende ◽  
Eliara Acipreste Hudson ◽  
Hauster Maximiler Campos de Paula ◽  
Yara Luiza Coelho ◽  
Luis Henrique Mendes da Silva ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Complex Formation ◽  
Fluorescence Spectroscopy ◽  
Comparative Study ◽  
Kinetic Study ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Bovine Lactoferrin

scholarly journals Study on complex formation between recombinant human thrombomodulin fragment and thrombin using surface plasmon resonance

2000 ◽  
Vol 63 (3) ◽  
pp. 136-140 ◽  
Author(s):  
Akio Kishida ◽  
Mihoko Nakashima ◽  
Nobuyuki Sakamoto ◽  
Takeshi Serizawa ◽  
Ikuro Maruyama ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Complex Formation ◽  
Surface Plasmon ◽  
Plasmon Resonance

scholarly journals Kinetic and Thermodynamic Analysis of Dimerization Inhibitors Binding to HIV Protease Monomers by Surface Plasmon Resonance

2012 ◽  
Vol 58 (1) ◽  
pp. 43-49 ◽  
Author(s):  
P.V. Ershov ◽  
O.V. Gnedenko ◽  
A.A. Molnar ◽  
A.V. Lisitsa ◽  
A.S. Ivanov ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Complex Formation ◽  
Thermodynamic Parameters ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Hiv Protease ◽  
Kinetic And Thermodynamic Parameters ◽  
Kinetic And Thermodynamic Analysis ◽  
Kinetic Equilibrium ◽  
Dimerization Inhibitors

Here, we describe the analysis of kinetic and thermodynamic parameters for binding of peptide and nonpeptide dimerization inhibitors to immobilized HIV protease (HIVp) monomers by using surface plasmon resonance. Molecular interactions were investigated at different inhibitors concentrations (0-80 μM) and temperatures (15-35°C). The kinetic, equilibrium and thermodynamic parameters have been determined. It was found that both inhibitors were characterized by similar interaction parameters. The complex formation is entropically driven process for both inhibitors. The entropic term(-ТΔS) had the value about -20 kcal/mol while the enthalpic term (ΔH) had the positive value about 14 kcal/mol and counteracted the complex formation.

The oligomeric state, complex formation, and chaperoning activity of Hsp70 and Hsp80 of Neurospora crassa

2002 ◽  
Vol 80 (6) ◽  
pp. 797-809 ◽  
Author(s):  
M E Britton ◽  
M Kapoor
Keyword(s):  
Surface Plasmon Resonance ◽  
Light Scattering ◽  
Complex Formation ◽  
Dynamic Light Scattering ◽  
Neurospora Crassa ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Molecular Chaperones ◽  
Citrate Synthase ◽  
Oligomeric State

Molecular chaperones perform vital cellular functions under normal growth conditions and protect cells against stress-induced damage. The stress proteins Hsp70 and Hsp80 of Neurospora crassa were extracted from heat-shocked mycelium, purified to near homogeneity, and examined with respect to their oligomeric state, complex formation, and chaperoning properties. Their oligomeric state was assessed by dynamic light-scattering measurements, and both Hsp70 and Hsp80 were observed to form a range of soluble, high-molecular-mass protein aggregates. Direct interaction between Hsp70 and Hsp80 was studied by partial tryptic digestion and surface plasmon resonance (SPR). Hsp70 was immobilized on the sensor chip surface, and the binding of Hsp80 in solution was followed in real time. Proteolytic digestion revealed that Hsp70–Hsp80 complex formation results in conformational changes in both proteins. The data from SPR studies yielded an equilibrium dissociation constant, KD, of 8.5 × 10–9 M. The chaperoning ability of Hsp70, Hsp80, and Hsp70–Hsp80 was monitored in vitro by the protection of citrate synthase from thermal aggregation. The binding of nucleotides modulates the oligomeric state, chaperoning function, and hetero-oligomeric complex formation of Hsp70 and Hsp80.Key words: molecular chaperones, surface plasmon resonance, dynamic light scattering, trypsin digestion, citrate synthase, Neurospora crassa.

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