skip to main content

Language:

N‐Terminal Cu‐Binding Motifs (Xxx‐Zzz‐His, Xxx‐His) and Their Derivatives: Chemistry, Biology and Medicinal Applications

Gonzalez, Paulina ; Bossak, Karolina ; Stefaniak, Ewelina ; Hureau, Christelle ; Raibaut, Laurent ; Bal, Wojciech ; Faller, Peter

Chemistry : a European journal, 2018-06, Vol.24 (32), p.8029-8041 [Peer Reviewed Journal]

Germany: Wiley Subscription Services, Inc

Full text available

Citations Cited by

Actions
1. Add to e-Shelf
2. Remove from e-Shelf
3. E-mail
4. Print
5. Permalink
6. Citation
7. EasyBib
8. EndNote
9. RefWorks
10. Delicious
11. Export RIS
12. Export BibTeX

Title:
N‐Terminal Cu‐Binding Motifs (Xxx‐Zzz‐His, Xxx‐His) and Their Derivatives: Chemistry, Biology and Medicinal Applications
Author: Gonzalez, Paulina ; Bossak, Karolina ; Stefaniak, Ewelina ; Hureau, Christelle ; Raibaut, Laurent ; Bal, Wojciech ; Faller, Peter
Subjects: Activation ; Affinity ; Alzheimer's disease ; amino acids ; Anticancer properties ; Antioxidants ; Binding Sites ; Chelation ; Chemical properties ; Chemical Sciences ; Chemistry ; Coordination chemistry ; Coordination Complexes - chemistry ; Copper - chemistry ; copper complexes ; Electron Spin Resonance Spectroscopy ; Medicinal Chemistry ; metallopeptides ; motifs ; Neurodegeneration ; Neurodegenerative diseases ; Nuclease ; Oligopeptides - chemistry ; Organic chemistry ; Oxidation-Reduction ; Peptides ; Positron emission ; Positron emission tomography ; Protein Binding ; Protein Conformation ; Proteins ; Serum albumin ; Tomography ; Wound healing
Is Part Of: Chemistry : a European journal, 2018-06, Vol.24 (32), p.8029-8041
Notes: ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
Description: Peptides and proteins with N‐terminal amino acid sequences NH2‐Xxx‐His (XH) and NH2‐Xxx‐Zzz‐His (XZH) form well‐established high‐affinity CuII‐complexes. Key examples are Asp‐Ala‐His (in serum albumin) and Gly‐His‐Lys, the wound healing factor. This opens a straightforward way to add a high‐affinity CuII‐binding site to almost any peptide or protein, by chemical or recombinant approaches. Thus, these motifs, NH2‐Xxx‐Zzz‐His in particular, have been used to equip peptides and proteins with a multitude of functions based on the redox activity of Cu, including nuclease, protease, glycosidase, or oxygen activation properties, useful in anticancer or antimicrobial drugs. More recent research suggests novel biological functions, mainly based on the redox inertness of CuII in XZH, like PET imaging (with 64Cu), chelation therapies (for instance in Alzheimer's disease and other types of neurodegeneration), antioxidant units, Cu transporters and activation of biological functions by strong CuII binding. This Review gives an overview of the chemical properties of Cu‐XH and ‐XZH motifs and discusses the pros and cons of the vastly different biological applications, and how they could be improved depending on the application. Paving the CuII‐way: Adding to peptides or proteins a histidine preceded by one or two amino acids at the N‐terminus yields a well‐established quite strong CuII‐binding site. This is easily achieved by chemical or recombinant means, and hence was exploited to engineer Cu‐sites into diverse peptides and proteins to add new biological and medical functions, like imaging, Cu‐redox silencing, biomolecule degradation, antibacterial and other activities.
Publisher: Germany: Wiley Subscription Services, Inc
Language: English

Links

Back to results list

Result 1 Next Go to Next page

Go to Next page

Implemented by: Social Network Logos:

Searching Remote Databases, Please Wait

Searching for
inscope:(USP_VIDEOS),scope:("PRIMO"),scope:(USP_FISICO),scope:(USP_EREVISTAS),scope:(USP),scope:(USP_EBOOKS),scope:(USP_PRODUCAO),primo_central_multiple_fe
Show me what you have so far