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Macromolecularization of a tripeptide analog of the Cu(II) binding site of human serum albumin. I. Synthesis, conformation, and binding properties of a Gly-Gly-His derivative of poly(L-lysine)

โœ Scribed by L. Michielin; S. Mammi; E. Peggion

Publisher
Wiley (John Wiley & Sons)
Year
1984
Tongue
English
Weight
34 KB
Volume
23
Category
Article
ISSN
0006-3525

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Macromolecularization of a tripeptide an
Macromolecularization of a tripeptide analog of the Cu(II) binding site of human serum albumin. I. Synthesis, conformation, and binding properties of a Gly-Gly-His derivative of poly(L-lysine)
โœ L. Michielin; S. Mammi; E. Peggion ๐Ÿ“‚ Article ๐Ÿ“… 1983 ๐Ÿ› Wiley (John Wiley & Sons) ๐ŸŒ English โš– 227 KB ๐Ÿ‘ 1 views

The Cu(I1) binding site of human serum albumin is located on the N-terminal sequence Asp-Ala-His.l-4 It has been shown that the synthetic tripeptide Asp-Ala-His N-methylamide exhibits an affinity towards Cu(I1) ions even higher than that of serum albumin itself.5 In general, i t has been observed th