2016
DOI: 10.1590/s1984-82502016000300010
|View full text |Cite
|
Sign up to set email alerts
|

Characteristics and thermodynamics of the interaction of 6-shogaol with human serum albumin as studied by isothermal titration calorimetry

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

0
1
0

Year Published

2020
2020
2023
2023

Publication Types

Select...
5

Relationship

0
5

Authors

Journals

citations
Cited by 7 publications
(1 citation statement)
references
References 16 publications
(15 reference statements)
0
1
0
Order By: Relevance
“…[ 25 ] In our studied system, the Δ H of this first equilibrium was high, Δ H = (–6.69 ± 0.05) × 10 4 cal mol –1 , indicating that another kind of binding was acting together with the electrostatic binding. This extra energy registered could correspond to hydrogen bonding between the head of the CTAB molecules and the rhEGF protein [ 26 ] or a reorganization of the rhEGF structure upon contact with the Blank@Quatsomes. As was previously evidenced by both CD and intrinsic Trp fluorescence, aromatic amino acids are probably implicated in rhEGF binding to the quatsome surface.…”
Section: Resultsmentioning
confidence: 99%
“…[ 25 ] In our studied system, the Δ H of this first equilibrium was high, Δ H = (–6.69 ± 0.05) × 10 4 cal mol –1 , indicating that another kind of binding was acting together with the electrostatic binding. This extra energy registered could correspond to hydrogen bonding between the head of the CTAB molecules and the rhEGF protein [ 26 ] or a reorganization of the rhEGF structure upon contact with the Blank@Quatsomes. As was previously evidenced by both CD and intrinsic Trp fluorescence, aromatic amino acids are probably implicated in rhEGF binding to the quatsome surface.…”
Section: Resultsmentioning
confidence: 99%