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Inside Back Cover: Allosteric Modulation of Human Serum Albumin Induced by Peptide Ligand (Chin. J. Chem. 8/2017)
Author(s) -
Hou Jingfei,
Peng Jiaxi,
Yu Yue,
Lin Yuchen,
Liu Changliang,
Duan Hongyang,
Yang Yanlian,
Wang Chen
Publication year - 2017
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.201770084
Subject(s) - chemistry , allosteric regulation , human serum albumin , peptide , ligand (biochemistry) , allosteric modulator , biophysics , stereochemistry , biochemistry , receptor , biology
The inside back cover picture shows the allosteric modulation of human serum albumin (HSA) induced by the Peptide SA06 ligand. Peptide SA06 is a reported peptide ligand comprising 20 amino acids, and is known to non‐covalently bind with HSA to extend the lifetime and improve the pharmacokinetic performance of drug molecules. The structural evidence on the allosteric interaction between peptide ligand and HSA, and the structure‐affinity relations of the binding mechanism have been revealed in this work, which can also shed light on optimization of therapeutic properties in the affinity‐controlled delivery systems. More details are discussed in the article by Wang et al. on page 1270–1277.