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‫أروى ﺣﺴﻦ اﻟﻔﻘﻴﻪ‬

chlorogenic acid

MOLECULAR FORMULA
M.W Logp TPSA Enzyme Effect on pepsin
inhibito
r

li Liang, ‐jin Zeng, Hui‐Hua

C16H18O9 354.31 0.45- 164.74 0.62
bo qu ‐Jing You, Ling
Luminescence 29 (7)
,(2014 ,715-721

Study on the binding of chlorogenic acid to pepsin by spectral and molecular docking

interaction of pepsin with chlorogenic acid (CHA) was investigated using The
fluorescence, UV/vis spectroscopy and molecular modeling methods. Stern–Volmer
analysis indicated that the fluorescence quenching of pepsin by CHA resulted from a
static mechanism, and the binding constant was 1.1846 × 105 and 1.1587 × 105
L/mol at 288 and 310 K, respectively. The distance between donor (pepsin) and
acceptor (CHA) was calculated to be 2.39 nm and the number of binding sites for
CHA binding on pepsin was ~ 1. The results of synchronous fluorescence and
three‐dimensional fluorescence showed that binding of CHA to pepsin could induce
conformational changes in pepsin. Molecular docking experiments found that CHA
bonded with pepsin in the area of the hydrophobic cavity with Van der Waals' forces
or hydrogen bonding interaction, which were consistent with the results obtained
from the thermodynamic parameter analysis.

.Furthermore, the binding of CHA can inhibit pepsin activity in vitro