Skip to main content

Technetium-binding in labelled HYNIC-peptide conjugates: Role of coordinating amino acids

Surfraz, M.B.-U., King, R., Mather, S.J., Biagini, S.C.G., Blower, P.J. (2009) Technetium-binding in labelled HYNIC-peptide conjugates: Role of coordinating amino acids. Journal of Inorganic Biochemistry, 103 (7). pp. 971-977. ISSN 01620134 (ISSN). (doi:10.1016/j.jinorgbio.2009.04.007) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
http://www.scopus.com/inward/record.url?eid=2-s2.0...

Abstract

Electrospray mass spectrometry (ESMS) of certain peptides labelled with 99mTc via hydrazinonicotinamide (HYNIC) with tricine as co-ligand shows one Tc-bound tricine, whereas typically two are observed. We speculated that this was due to coordination of a neighbouring histidine (His) or glutamate (Glu). To investigate this possibility, several short peptides incorporating lysine (HYNIC), with and without His and Glu at different positions in the sequence, were radiolabelled with 99mTc, using tricine, ethylenediaminediacetic acid (EDDA) and nicotinic acid as co-ligands. The products were examined by HPLC-ESMS, cysteine challenge and bovine serum albumin (BSA) challenge. Peptides with His nearby on either side of lysine (HYNIC) contained only one tricine and showed markedly enhanced structural homogeneity and stability to cysteine challenge and BSA binding, except those with His located at the N-terminus. Peptides without His, or with neighbouring N-terminal His, contained two tricines and were less stable to cysteine challenge and BSA binding. Glu participated in Tc-binding but did not enhance stability. We conclude that neighbouring His or Glu side chains coordinate to Tc and this could alter peptide or protein conformation. Inclusion of His in a neighbouring position to lysine (HYNIC) enhances stability, improves homogeneity and reduces the demand of the metal center for binding to additional co-ligands. © 2009 Elsevier Inc. All rights reserved.

Item Type: Article
DOI/Identification number: 10.1016/j.jinorgbio.2009.04.007
Additional information: Unmapped bibliographic data: LA - English [Field not mapped to EPrints] J2 - J. Inorg. Biochem. [Field not mapped to EPrints] C2 - 19447500 [Field not mapped to EPrints] AD - Cancer Research Group, Biosciences Dept., University of Kent, Canterbury, Kent CT2 7NJ, United Kingdom [Field not mapped to EPrints] AD - Cancer Research UK, Department of Nuclear Medicine, St. Bartholomew's Hospital, London, EC1A 7BE, United Kingdom [Field not mapped to EPrints] AD - Functional Materials Group, School of Physical Sciences, University of Kent, Canterbury, CT2 7NJ, United Kingdom [Field not mapped to EPrints] AD - Kings College London, Division of Imaging Sciences, Rayne Institute, 4th Floor Lambeth Wing, London, SE1 7EH, United Kingdom [Field not mapped to EPrints] DB - Scopus [Field not mapped to EPrints]
Uncontrolled keywords: HYNIC, Peptides, Radiopharmaceuticals, Technetium-99m, acetic acid derivative, amino acid derivative, bovine serum albumin, coordination compound, cysteine, glutamic acid, histidine, hydrazinonicotinamide, lysine, nicotinamide derivative, nicotinic acid, peptide, peptide derivative, technetium 99m, unclassified drug, amino terminal sequence, article, isotope labeling, ligand binding, protein conformation, protein stability, Animals, Cattle, Glutamic Acid, Glycine, Histidine, Hydrazines, Niacinamide, Peptides, Serum Albumin, Bovine, Spectrometry, Mass, Electrospray Ionization, Technetium, Bovinae
Subjects: Q Science > QD Chemistry > QD431 Organic Chemistry- Biochemistry- Proteins, peptides, amino acids
R Medicine > R Medicine (General) > R895 Nuclear Medicine
Divisions: Faculties > Sciences > School of Physical Sciences > Functional Materials Group
Depositing User: Giles Tarver
Date Deposited: 21 Jul 2015 10:56 UTC
Last Modified: 29 May 2019 14:52 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/49614 (The current URI for this page, for reference purposes)
  • Depositors only (login required):