A minimalist chemical model of matrix metalloproteinases- Can small peptides mimic the more rigid metal binding sites of proteins?
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Tartalom: http://www.ncbi.nlm.nih.gov/pubmed/23787141
Archívum: MTA Könyvtár
Gyűjtemény: Status = Unpublished


Type = Article
Cím:
A minimalist chemical model of matrix metalloproteinases- Can small peptides mimic the more rigid metal binding sites of proteins?
Létrehozó:
Árus, Dávid
Nagy, Nóra Veronika
Dancs, Ágnes
Jancsóc, Attila
Berkecz, Róbert
Gajda, Tamás
Kiadó:
Elsevier
Dátum:
2013
Téma:
QD Chemistry / kémia
QD03 Inorganic chemistry / szervetlen kémia
Tartalmi leírás:
In order to develop a minimalist chemical model of matrix metalloproteinases (MMPs), we
synthesized a pentadecapeptide (Ac-KAHEFGHSLGLDHSK-NH2) corresponding to the
catalytic zinc(II) binding site of human MMP-13. The multi-domain structural organization of
MMPs fundamentally determines their metal binding affinity, catalytic activity and
selectivity. Our potentiometric, UV-VIS, CD, EPR, NMR, ESI-MS and kinetic study are
aimed to explore the usefulness of flexible peptides to mimic the more rigid metal binding
sites of proteins, to examine the intrinsic metal binding properties of this naked sequence, as
well as to contribute the development of a minimalist, peptide-based chemical model of
MMPs, including the catalytic properties. Since multiimidazole environment is also
characteristic for copper(II), and recently copper(II) containing variants of MMPs have been
identified, we also studied the copper(II) complexes of the above peptide.
Around pH 6-7 the peptide, similarly to MMPs, offers (3Nim) coordinated binding site
for both zinc(II) and copper(II). In the case of copper(II), the formation of amide coordinated
species at higher pH ceased the analogy with the copper(II) containing MMP variant. On the
other hand, the zinc(II)-peptide system mimics some basic features of the MMP active sites:
the main species around pH 7 (ZnH2L) possesses (3Nim,H2O) coordination environment, the
deprotonation of the zinc-bound water takes place near to the physiological pH, it forms
relatively stable ternary complexes with hydroxamic acids, and the species ZnH2L(OH) and
ZnH2L(OH)2 have notable hydrolytic activity between pH 7-9.
Típus:
Article
NonPeerReviewed
Formátum:
text
Azonosító:
Árus, Dávid and Nagy, Nóra Veronika and Dancs, Ágnes and Jancsóc, Attila and Berkecz, Róbert and Gajda, Tamás (2013) A minimalist chemical model of matrix metalloproteinases- Can small peptides mimic the more rigid metal binding sites of proteins? Jorunal of Inorganic Biochemistry, 126. pp. 61-69. ISSN 0162-0134 (Unpublished)
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