The critical role of dimer formation in monosaccharides binding to human serum albumin

2018 ◽  
Vol 20 (5) ◽  
pp. 3249-3257 ◽  
Author(s):  
Prapasiri Pongprayoon ◽  
Toshifumi Mori
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Critical Role ◽  
Binding Pocket ◽  
Dimer Formation ◽  
Dimeric Structure

Monosaccharides are found to bind tightly to human serum albumin when a dimeric structure is formed in the binding pocket.

scholarly journals Role of Gingipains in Growth of Porphyromonas gingivalis in the Presence of Human Serum Albumin

2001 ◽  
Vol 69 (8) ◽  
pp. 5166-5172 ◽  
Author(s):  
Daniel Grenier ◽  
Sandra Imbeault ◽  
Pascale Plamondon ◽  
Gilbert Grenier ◽  
Koji Nakayama ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Porphyromonas Gingivalis ◽  
Parent Strain ◽  
Proteolytic Enzymes ◽  
Protein Hydrolysate ◽  
Critical Role ◽  
Defined Medium

ABSTRACT Porphyromonas gingivalis, a bacterium associated with active chronic periodontitis lesions, produces several proteolytic enzymes that are thought to be involved in host colonization, perturbation of the immune system, and tissue destruction. The aim of the present study was to investigate the contribution of Arg- and Lys-gingipains produced by P. gingivalis to its growth. Although all of the proteins studied were degraded by P. gingivalis, only human serum albumin and transferrin supported growth during serial transfers in a chemically defined medium (CDM). Growth studies with site-directed gingipain-deficient mutants ofP. gingivalis revealed that inactivation of both gingipains prevents growth, whereas inactivation of either Arg- or Lys-gingipain activity extended the doubling times to 33 or 13 h, respectively, compared to 9 h for the parent strain. Growth of the mutants and the parent strain was similar when the CDM was supplemented with a protein hydrolysate instead of human serum albumin. Incubation of resting P. gingivalis ATCC 33277 cells with fluorophore-labeled albumin indicated that the proteolytic fragments generated by the gingipains were internalized by the bacterial cells. Internalization of fluorophore-labeled albumin fragments was reduced or completely inhibited in the proteinase-deficient mutants. Interestingly, gingival crevicular fluid samples from diseased periodontal sites contained low-molecular-mass albumin fragments, whereas samples from healthy sites did not. The critical role of proteinases in the growth of P. gingivalis was further investigated using specific Arg- and Lys-gingipain inhibitors. Adding the inhibitors to CDM containing albumin revealed that leupeptin (Arg-gingipain A and B inhibitor) was more efficient at inhibiting growth than cathepsin B inhibitor II (Lys-gingipain inhibitor). Our study suggests that Arg-gingipains and, to a lesser extent, Lys-gingipain play an important role in the growth of P. gingivalis in a defined medium containing a human protein as the sole carbon and nitrogen source.

scholarly journals Reversible Dimerization of Human Serum Albumin

Molecules ◽  
2020 ◽  
Vol 26 (1) ◽  
pp. 108
Author(s):  
Alexey Chubarov ◽  
Anna Spitsyna ◽  
Olesya Krumkacheva ◽  
Dmitry Mitin ◽  
Daniil Suvorov ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Spin Labels ◽  
Dimer Formation ◽  
Paramagnetic Resonance ◽  
Post Translational Modifications ◽  
Physiological Processes ◽  
Reversible Dimerization

Pulsed Dipolar Spectroscopy (PDS) methods of Electron Paramagnetic Resonance (EPR) were used to detect and characterize reversible non-covalent dimers of Human Serum Albumin (HSA), the most abundant protein in human plasma. The spin labels, MTSL and OX063, were attached to Cys-34 and these chemical modifications of Cys-34 did affect the dimerization of HSA, indicating that other post-translational modifications can modulate dimer formation. At physiologically relevant concentrations, HSA does form weak, non-covalent dimers with a well-defined structure. Dimer formation is readily reversible into monomers. Dimerization is very relevant to the role of HSA in the transport, binding, and other physiological processes.

scholarly journals Role of cationic carbosilane dendrons and metallic core of functionalized gold nanoparticles in their interaction with human serum albumin

2018 ◽  
Vol 118 ◽  
pp. 1773-1780 ◽  
Author(s):  
Dzmitry Shcharbin ◽  
Elzbieta Pedziwiatr-Werbicka ◽  
Tatyana Serchenya ◽  
Sylwia Cyboran-Mikolajczyk ◽  
Lena Prakhira ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Metallic Core ◽  
Functionalized Gold Nanoparticles

Role of surface charge on the interaction between carbon nanodots and human serum albumin

2018 ◽  
Vol 204 ◽  
pp. 484-494 ◽  
Author(s):  
Meng-Ying Li ◽  
Chang-Qing Xiao ◽  
Zi-Qiang Xu ◽  
Miao-Miao Yin ◽  
Qi-Qi Yang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Surface Charge ◽  
Carbon Nanodots

Binding of cationic Cm-E2O-Cm gemini surfactants with human serum albumin and the role of β-cyclodextrin

2020 ◽  
Vol 312 ◽  
pp. 113365 ◽  
Author(s):  
Mohd. Akram ◽  
Farah Ansari ◽  
Faizan Abul Qais ◽  
Kabir-ud-Din
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gemini Surfactants

The role of human serum albumin and neurotoxin associated proteins in the formulation of BoNT/A products

Toxicon ◽  
2019 ◽  
Vol 168 ◽  
pp. 158-163 ◽  
Author(s):  
Anna Kutschenko ◽  
Hans Bigalke ◽  
Florian Wegner ◽  
Kai Wohlfarth
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Associated Proteins
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