How trimerization of CTR1 N-terminal model peptides tunes Cu-binding and redox-chemistry

Thibaut Galler; Vincent Lebrun; Laurent Raibaut; Peter Faller; Nina E. Wezynfeld

doi:10.1039/d0cc04693k

How trimerization of CTR1 N-terminal model peptides tunes Cu-binding and redox-chemistry

Chemical Communications ◽

10.1039/d0cc04693k ◽

2020 ◽

Vol 56 (81) ◽

pp. 12194-12197

Author(s):

Thibaut Galler ◽

Vincent Lebrun ◽

Laurent Raibaut ◽

Peter Faller ◽

Nina E. Wezynfeld

Keyword(s):

Redox Chemistry ◽

N Terminus ◽

Terminal Model ◽

Model Peptides

Trimeric arrangement of model peptides of the CTR1 N-terminus promotes Cu(ii) reduction and Cu(i) binding.

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Glutathione peroxidase: Redox chemistry of active site model peptides

Bioorganic & Medicinal Chemistry Letters ◽

10.1016/s0960-894x(01)81042-8 ◽

1991 ◽

Vol 1 (5) ◽

pp. 277-280 ◽

Cited By ~ 6

Author(s):

P. Chan ◽

P. Cotelle ◽

N. Cotelle ◽

J.L. Bernier ◽

J.P. Hénichart

Keyword(s):

Glutathione Peroxidase ◽

Active Site ◽

Redox Chemistry ◽

Site Model ◽

Active Site Model ◽

Model Peptides

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Alpha Helix Nucleation by a Simple Cyclic Tetrapeptide

Australian Journal of Chemistry ◽

10.1071/ch16591 ◽

2017 ◽

Vol 70 (2) ◽

pp. 213 ◽

Cited By ~ 4

Author(s):

Huy N. Hoang ◽

Chongyang Wu ◽

Renee L. Beyer ◽

Timothy A. Hill ◽

David P. Fairlie

Keyword(s):

Alpha Helix ◽

Biologically Relevant ◽

Helical Peptide ◽

Helix Nucleation ◽

Helix Capping ◽

N Terminus ◽

Turn Structure ◽

Cyclic Tetrapeptide ◽

Model Peptides

The simple cyclic tetrapeptide cyclo-(1,4)-[Ala-Arg-Ala-homoGlu]-NH2 (3) is shown to adopt an unusual α-turn structure, which is not α-helical but can nucleate α-helicity when attached to the N-terminus of either model peptides or two biologically relevant peptides. This new N-terminal helix-capping macrocycle provides very simple and rapid synthetic access to α-helical peptide structures.

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Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II

Biopolymers ◽

10.1002/bip.20374 ◽

2006 ◽

Vol 84 (2) ◽

pp. 169-180 ◽

Cited By ~ 42

Author(s):

Fábio Casallanovo ◽

Felipe J. F. de Oliveira ◽

Fernando C. de Souza ◽

Uris Ros ◽

Yohanka Martínez ◽

...

Keyword(s):

Structure And Function ◽

N Terminus ◽

And Function ◽

Model Peptides

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NMR Studies of Model Peptides of PHGGGWGQ Repeats within the N-Terminus of Prion Proteins: A Loop Conformation with Histidine and Tryptophan in Close Proximity

The Journal of Biochemistry ◽

10.1093/oxfordjournals.jbchem.a022750 ◽

2000 ◽

Vol 128 (2) ◽

pp. 271-281 ◽

Cited By ~ 19

Author(s):

H. Yoshida ◽

N. Matsushima ◽

Y. Kumaki ◽

M. Nakata ◽

K. Hikichi

Keyword(s):

Prion Proteins ◽

Nmr Studies ◽

Close Proximity ◽

N Terminus ◽

Loop Conformation ◽

Model Peptides

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Characteristics of the Interaction between Thrombin Exosite1 and the Sequence 269-297 of Platelet Glycoprotein Ibα

Thrombosis and Haemostasis ◽

10.1055/s-0037-1615193 ◽

1998 ◽

Vol 80 (08) ◽

pp. 310-315 ◽

Cited By ~ 8

Author(s):

Marie-Christine Bouton ◽

Christophe Thurieau ◽

Marie-Claude Guillin ◽

Martine Jandrot-Perrus

Keyword(s):

Platelet Activation ◽

Electrostatic Interactions ◽

Platelet Glycoprotein ◽

Thrombin Receptor ◽

Central Position ◽

Amidolytic Activity ◽

N Terminus ◽

Hydrolysis Of ◽

Chemical Cross Linking ◽

Positively Charged

SummaryThe interaction between GPIb and thrombin promotes platelet activation elicited via the hydrolysis of the thrombin receptor and involves structures located on the segment 238-290 within the N-terminal domain of GPIbα and the positively charged exosite 1 on thrombin. We have investigated the ability of peptides derived from the 269-287 sequence of GPIbα to interact with thrombin. Three peptides were synthesized, including Ibα 269-287 and two scrambled peptides R1 and R2 which are comparable to Ibα 269-287 with regards to their content and distribution of anionic residues. However, R2 differs from both Ibα 269-287 and R1 by the shifting of one proline from a central position to the N-terminus. By chemical cross-linking, we observed the formation of a complex between 125I-Ibα 269-287 and α-thrombin that was inhibited by hirudin, the C-terminal peptide of hirudin, sodium pyrophosphate but not by heparin. The complex did not form when γ-thrombin was substituted for α-thrombin. Ibα 269-287 produced only slight changes in thrombin amidolytic activity and inhibited thrombin binding to fibrin. R1 and R2 also formed complexes with α-thrombin, modified slightly its catalytic activity and inhibited its binding to fibrin. Peptides Ibα 269-287 and R1 inhibited platelet aggregation and secretion induced by low thrombin concentrations whereas R2 was without effect. Our results indicate that Ibα 269-287 interacts with thrombin exosite 1 via mainly electrostatic interactions, which explains why the scrambled peptides also interact with exosite 1. Nevertheless, the lack of effect of R2 on thrombin-induced platelet activation suggests that proline 280 is important for thrombin interaction with GPIb.

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