scholarly journals Gas phase noncovalent protein complexes that retain solution binding properties: Binding of xylobiose inhibitors to the β-1, 4 exoglucanase from Cellulomonas fimi

2007 ◽  
Vol 18 (1) ◽  
pp. 64-73 ◽  
Author(s):  
Milica Tešić ◽  
Jacqueline Wicki ◽  
David K. Y. Poon ◽  
Stephen G. Withers ◽  
Donald J. Douglas
Keyword(s):  
Gas Phase ◽  
Protein Complexes ◽  
Binding Properties ◽  
Cellulomonas Fimi ◽  
Noncovalent Protein

Extended Gas-Phase Trapping Followed by Surface-Induced Dissociation of Noncovalent Protein Complexes

2015 ◽  
Vol 88 (2) ◽  
pp. 1218-1221 ◽  
Author(s):  
Sophie R. Harvey ◽  
Jing Yan ◽  
Jeffery M. Brown ◽  
Emmy Hoyes ◽  
Vicki H. Wysocki
Keyword(s):  
Gas Phase ◽  
Protein Complexes ◽  
Surface Induced Dissociation ◽  
Noncovalent Protein

Gas Phase Stabilization of Noncovalent Protein Complexes Formed by Electrospray Ionization

2009 ◽  
Vol 81 (18) ◽  
pp. 7801-7806 ◽  
Author(s):  
Dhanashri Bagal ◽  
Elena N. Kitova ◽  
Lan Liu ◽  
Amr El-Hawiet ◽  
Paul D. Schnier ◽  
...  
Keyword(s):  
Electrospray Ionization ◽  
Gas Phase ◽  
Protein Complexes ◽  
Phase Stabilization ◽  
Noncovalent Protein

Symmetrical Gas-Phase Dissociation of Noncovalent Protein Complexes via Surface Collisions

2006 ◽  
Vol 128 (47) ◽  
pp. 15044-15045 ◽  
Author(s):  
Christopher M. Jones ◽  
Richard L. Beardsley ◽  
Asiri S. Galhena ◽  
Shai Dagan ◽  
Guilong Cheng ◽  
...  
Keyword(s):  
Gas Phase ◽  
Protein Complexes ◽  
Noncovalent Protein ◽  
Gas Phase Dissociation

Paper Spray Ionization of Noncovalent Protein Complexes

2014 ◽  
Vol 86 (3) ◽  
pp. 1342-1346 ◽  
Author(s):  
Yun Zhang ◽  
Yue Ju ◽  
Chengsi Huang ◽  
Vicki H. Wysocki
Keyword(s):  
Protein Complexes ◽  
Paper Spray ◽  
Paper Spray Ionization ◽  
Noncovalent Protein

scholarly journals Design and Characterisation of Inhibitory Peptides against Bleg1_2478, an Evolutionary Divergent B3 Metallo-β-lactamase

Molecules ◽  
2020 ◽  
Vol 25 (24) ◽  
pp. 5797
Author(s):  
Gayathri Selvaraju ◽  
Thean Chor Leow ◽  
Abu Bakar Salleh ◽  
Yahaya M. Normi
Keyword(s):  
Active Site ◽  
Protein Complexes ◽  
Hypothetical Protein ◽  
Titration Calorimetry ◽  
Binding Properties ◽  
Vitro Assay ◽  
In Silico Docking ◽  
Inhibitory Peptides ◽  
Catalytic Function

Previously, a hypothetical protein (HP) termed Bleg1_2437 (currently named Bleg1_2478) from Bacillus lehensis G1 was discovered to be an evolutionary divergent B3 subclass metallo-β-lactamase (MBL). Due to the scarcity of clinical inhibitors for B3 MBLs and the divergent nature of Bleg1_2478, this study aimed to design and characterise peptides as inhibitors against Bleg1_2478. Through in silico docking, RSWPWH and SSWWDR peptides with comparable binding energy to ampicillin were obtained. In vitro assay results showed RSWPWH and SSWWDR inhibited the activity of Bleg1_2478 by 50% at concentrations as low as 0.90 µM and 0.50 µM, respectively. At 10 µM of RSWPWH and 20 µM of SSWWDR, the activity of Bleg1_2478 was almost completely inhibited. Isothermal titration calorimetry (ITC) analyses showed slightly improved binding properties of the peptides compared to ampicillin. Docked peptide–protein complexes revealed that RSWPWH bound near the vicinity of the Bleg1_2478 active site while SSWWDR bound at the center of the active site itself. We postulate that the peptides caused the inhibition of Bleg1_2478 by reducing or blocking the accessibility of its active site from ampicillin, thus hampering its catalytic function.

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