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  Ion binding properties in acetonitrile of cyclo‐peptides built u from proline and glycine residues

Hollosi, M., & Wieland, T. (1977). Ion binding properties in acetonitrile of cyclo‐peptides built u from proline and glycine residues. International Journal Peptide Protein Research, 10(5), 329-341. doi:10.1111/j.1399-3011.1977.tb02805.x.

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IntJPeptProtRes_10_1977_329.pdf (Any fulltext), 605KB
 
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 Creators:
Hollosi, Miklos, Author
Wieland, Theodor1, Author           
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1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

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Free keywords: alkali metal complexes; alkaline earth metal complexes; CD‐spectra; complexones; cyclopeptides
 Abstract: Ion binding properties of antamanide‐like cyclopeptides cyclo‐(Pro2–Glyn‐Pro2–Glym) (n, m = 1–3) have been studied by CD spectroscopy and by conductivity measurements. Cyclo‐(Pro2–Gly‐Pro2–Gly) forming complexes of different stoichiometry can be characterized by a strong preference of selectivity for Mg++ and Ca++ ions over alkali ions whereas the other members of the series bind selectively alkali and alkaline earth cations with ion radius of about 1 Å. Three main types of CD spectra of cyclic peptides and their complexes can be differentiated. Type I showing two negative Cotton effects at around 220 nm and 200 nm (Ib, Fig. 3), type II showing a positive band around 220 nm and a strong negative one below 190 nm (e.g. Ic in acetonitrile, Fig. 4), and type III showing a strong negative band in the 205 nm region (e.g. metal complexes of Id, Fig. 6).

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Language(s): eng - English
 Dates: 1977-01-101977-06-011977-11
 Publication Status: Issued
 Pages: 13
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 Rev. Type: Peer
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Title: International Journal Peptide Protein Research
Source Genre: Journal
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Publ. Info: Copenhagen : Munksgaard
Pages: - Volume / Issue: 10 (5) Sequence Number: - Start / End Page: 329 - 341 Identifier: ISSN: 0367-8377
ISSN: 0300-9769