Uncapping the N-terminus of a ubiquitous His-tag peptide enhances its Cu2+ binding affinity

被引：8

作者：

Watly, J. ^{[1
]}

Hecel, A. ^{[1
]}

Wieczorek, R. ^{[1
]}

Swiatek-Korlowska, J. ^{[2
]}

Kozlowski, H. ^{[1
,2
]}

Rowinska-Zyrek, M. ^{[1
]}

机构：

[1] Univ Wroclaw, Fac Chem, F Joliot Curie 14, PL-50383 Wroclaw, Poland

[2] Publ Higher Med Profess Sch Opole, Katowicka 68, PL-45060 Opole, Poland

来源：

DALTON TRANSACTIONS | 2019年 / 48卷 / 36期

关键词：

SNAKE-VENOM METALLOPROTEINASES; COPPER(II); HISTIDINE; FAMILY; IONS; COORDINATION; COMPLEXES; CU(II); EQUILIBRIA; CONSTANTS;

D O I：

10.1039/c9dt01635j

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

Metal complexes with an N-terminally free and N-terminally acetylated polyhistidine region of Echis ocellatus venom, with an interesting His-rich motif present in numerous metal binding proteins from all kingdoms of life (DHDHDHHHHHHPGSSV-NH2 and Ac-DHDHDHHHHHHPGSSV-NH2) show the role of the free amino group in the thermodynamic enhancement of Cu2+, Ni2+ and Zn2+ binding. In the studied sequences, Cu2+ can be coordinated by different sets of imidazole rings, and a 3-10 helix is detected in close proximity of Cu2+ binding sites. The complexes are more stable than those with a typical His6-tag, despite a similar copper(II) coordination mode in both cases.

引用

页码：13567 / 13579

页数：13

共 22 条

[1] The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity
Chang, Chung-ke
Wu, Tzong-Huah
Wu, Chu-Ya
Chiang, Ming-hui
Toh, Elsie Khai-Woon
Hsu, Yin-Chih
Lin, Ku-Feng
Liao, Yu-heng
Huang, Tai-huang
Huang, Joseph Jen-Tse
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2012, 425 (02) : 219 - 224
[2] A Deeper Insight in Metal Binding to the hCtr1 N-terminus Fragment: Affinity, Speciation and Binding Mode of Binuclear Cu2+ and Mononuclear Ag+ Complex Species
Magri, Antonio
Tabbi, Giovanni
Naletova, Irina
Attanasio, Francesco
Arena, Giuseppe
Rizzarelli, Enrico
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2022, 23 (06)
[3] Novel immobilized Cu+2 ion grafted cellophane membranes for affinity separation of His-Tag Chitinase
Eldin, M. S. Mohy
Rahman, S. Abdel
El Fawal, G. F.
ARABIAN JOURNAL OF CHEMISTRY, 2017, 10 : S3652 - S3663
[4] Short polyglutamine peptide forms a high-affinity binding site for thioflavin-T at the N-terminus
Matsuoka, Shigeru
Murai, Motoki
Yamazaki, Toshio
Inoue, Masayuki
ORGANIC & BIOMOLECULAR CHEMISTRY, 2012, 10 (30) : 5787 - 5790
[5] Copper2+ Binding to α-Synuclein. Histidine50 Can Form a Ternary Complex with Cu2+ at the N-Terminus but Not a Macrochelate
Tian, Yao
Stanyon, Helen F.
Barritt, Joseph D.
Mayet, Uroosa
Patel, Pelak
Karamani, Elena
Fusco, Giuliana
Viles, John H.
INORGANIC CHEMISTRY, 2019, 58 (22) : 15580 - 15589
[6] THE N-TERMINUS OF NEUROHYPOPHYSIAL PEPTIDE HORMONE RECEPTORS: ITS ROLE IN HORMONE BINDING, LIGAND SELECTIVITY AND RECEPTOR ACTIVATION
Wheatley, M.
Hawtin, S. R.
Wesley, V. J.
Argent, C. C. H.
Simms, J.
JOURNAL OF PEPTIDE SCIENCE, 2004, 10 : 234 - 234
[7] Novel immobilized Cu2+-aminated poly (methyl methacrylate) grafted cellophane membranes for affinity separation of His-Tag chitinase
Mohy Eldin, M. S.
Abdel Rahman, S.
El Fawal, G. F.
POLYMER BULLETIN, 2020, 77 (01) : 135 - 151
[8] Novel immobilized Cu2+-aminated poly (methyl methacrylate) grafted cellophane membranes for affinity separation of His-Tag chitinase
M. S. Mohy Eldin
S. Abdel Rahman
G. F. El Fawal
Polymer Bulletin, 2020, 77 : 135 - 151
[9] Cu2+ reduces hemolytic activity of the antimicrobial peptide HMPI and enhances its trypsin resistance
Peng, Jinxiu
Yang, Yang
Zhao, Ping
Qiu, Shuai
Jia, Fengjing
Wang, Jiayi
Liang, Xiaolei
Chaudhry, Ahmed Shabbir
Xu, Peihan
Yan, Wenjin
Xu, Zhaoqing
Wang, Kairong
ACTA BIOCHIMICA ET BIOPHYSICA SINICA, 2020, 52 (06) : 603 - 611
[10] Oxysterol-binding protein (OSBP) enhances replication of intracellular Salmonella and binds the Salmonella SPI-2 effector SseL via its N-terminus
Auweter, Sigrid D.
Yu, Hong B.
Arena, Ellen T.
Guttman, Julian A.
Finlay, B. Brett
MICROBES AND INFECTION, 2012, 14 (02) : 148 - 154

← 1 2 3 →