ACS Publications. Most Trusted. Most Cited. Most Read
Ternary Cu2+ Complexes of Human Serum Albumin and Glycyl-l-histidyl-l-lysine

OR SEARCH CITATIONS

My Activity
Publications

Figure 1Loading Img
Download Hi-Res ImageDownload to MS-PowerPointCite This:Inorg. Chem. 2021, 60, 22, 16927-16931
    Communication

    Ternary Cu2+ Complexes of Human Serum Albumin and Glycyl-l-histidyl-l-lysine
    Click to copy article linkArticle link copied!

    Other Access OptionsSupporting Information (1)

    Inorganic Chemistry

    Cite this: Inorg. Chem. 2021, 60, 22, 16927–16931
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acs.inorgchem.1c03084
    Published November 3, 2021
    Copyright © 2021 American Chemical Society
    Request reuse permissions

    Abstract

    Click to copy section linkSection link copied!
    Abstract Image

    Human serum albumin (HSA) and the growth factor glycyl-l-histidyl-l-lysine (GHK) bind Cu2+ as part of their normal functions. GHK is found at its highest concentration in the albumin-rich fraction of plasma, leading to speculation that HSA and GHK form a ternary Cu2+ complex. Although preliminary evidence was presented 40 years ago, the structure and stability of such a complex have remained elusive. Here, we show that two ternary Cu(GHK)NImHSA complexes are formed between GHK and the imino nitrogen (NIm) of His side chains of HSA. We identified His3 as one site of ternary complex formation (conditional binding constant cKCu(GHK)NImHis3Cu(GHK) = 2900 M–1 at pH 7.4), with the second site (cKCu(GHK)NImHisXCu(GHK) = 1700 M–1) likely being supplied by either His128 or His510. Together with the established role of HSA as a molecular shuttle in the blood, these complexes may aid the transport of the exchangeable Cu2+ pool and the functional form of GHK.

    Copyright © 2021 American Chemical Society

    Subjects

    what are subjects

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. Add or change your institution or let them know you’d like them to include access.

    Supporting Information

    Click to copy section linkSection link copied!

    The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acs.inorgchem.1c03084.

    • Experimental methods, additional spectroscopic characterization, solvent accessibility analysis, additional DFT-optimized molecular structures and coordinates (PDF)

    Terms & Conditions

    Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses). Permission may be obtained from ACS for other uses through requests via the RightsLink permission system: http://pubs.acs.org/page/copyright/permissions.html.

    Cited By

    Click to copy section linkSection link copied!

    This article is cited by 10 publications.

    1. Pengrong An, Zixin Zhang, Jincan Yang, Tianming Wang, Zhuoyue Wang, Chun-Lin Sun, Chuanguang Qin, Jun Li. Ultrasensitive and Label-Free Detection of Copper Ions by GHK-Modified Asymmetric Nanochannels. Analytical Chemistry 2023, 95 (36) , 13456-13462. https://doi.org/10.1021/acs.analchem.3c01174
    2. Jessica A. San Juan, Khetpakorn Chakarawet, Zhecheng He, Rebeca L. Fernandez, Michael J. Stevenson, Nathaniel H. O. Harder, Samuel E. Janisse, Lee-Ping Wang, R. David Britt, Marie C. Heffern. Copper(II) Affects the Biochemical Behavior of Proinsulin C-peptide by Forming Ternary Complexes with Serum Albumin. Journal of the American Chemical Society 2023, 145 (30) , 16726-16738. https://doi.org/10.1021/jacs.3c04599
    3. Jin-Hong Min, Heela Sarlus, Robert A Harris. Glycyl- l -histidyl- l -lysine prevents copper- and zinc-induced protein aggregation and central nervous system cell death in vitro. Metallomics 2024, 16 (5) https://doi.org/10.1093/mtomcs/mfae019
    4. Justyna Żygowska, Marta Orlikowska, Igor Zhukov, Wojciech Bal, Aneta Szymańska. Copper interaction with cystatin C: effects on protein structure and oligomerization. The FEBS Journal 2024, 291 (9) , 1974-1991. https://doi.org/10.1111/febs.17092
    5. Martin Schaier, Enrico Falcone, Tomas Prstek, Bertrand Vileno, Sonja Hager, Bernhard K Keppler, Petra Heffeter, Gunda Koellensperger, Peter Faller, Christian R Kowol. Human serum albumin as a copper source for anticancer thiosemicarbazones. Metallomics 2023, 15 (8) https://doi.org/10.1093/mtomcs/mfad046
    6. Yongjuan Li, Ya Dong, Xinyao Zhou, Kelong Fan. Nanotechnology connecting copper metabolism and tumor therapy. MedComm – Biomaterials and Applications 2023, 2 (2) https://doi.org/10.1002/mba2.36
    7. Simon C. Drew. Chelator PBT2 Forms a Ternary Cu2+ Complex with β-Amyloid That Has High Stability but Low Specificity. International Journal of Molecular Sciences 2023, 24 (11) , 9267. https://doi.org/10.3390/ijms24119267
    8. Kexin Cao, Jingbing Zhang, Geng Wang, Xiaosheng Lin, Fulan Zhan, Kusheng Wu, Wei Tan, Hui Geng, Caixia Liu. Associations of trace element levels in paired serum, whole blood, and tissue: an example of esophageal squamous cell carcinoma. Environmental Science and Pollution Research 2023, 30 (13) , 38052-38062. https://doi.org/10.1007/s11356-022-24960-z
    9. Radosław Kotuniak, Wojciech Bal. Reactive Cu2+-peptide intermediates revealed by kinetic studies gain relevance by matching time windows in copper metallomics. Metallomics 2023, 15 (2) https://doi.org/10.1093/mtomcs/mfad007
    10. Yurong Luo, Hao Li, Muzhi Cai, Yuan Liu, Liang Chen, Shiqing Xu, Gongxun Bai. Designing polyacrylic acid capped luminescent rare earth core–shell nanoparticles for simultaneous Cu(II) and temperature sensing. Materials & Design 2022, 224 , 111405. https://doi.org/10.1016/j.matdes.2022.111405
    Download PDF
    Go to Inorganic Chemistry
    Get e-Alerts
    Get e-Alerts

    Inorganic Chemistry

    Cite this: Inorg. Chem. 2021, 60, 22, 16927–16931
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acs.inorgchem.1c03084
    Published November 3, 2021
    Copyright © 2021 American Chemical Society
    Request reuse permissions

    Article Views

    738

    Altmetric

    -

    Citations

    10
    Learn about these metrics

    Article Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.

    Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.

    The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated.