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(Cholestanyloxycarbonyl)benzyl esters as peptide substituents: Conformational properties of fully protected oligo‐ L ‐lysines with C‐terminal (cholestanyloxycarbonyl)benzyl and benzyl ester moieties
Author(s) -
Toniolo Claudio,
Bonora Gian Maria,
Moretto Vittorio,
Schneider Conrad H.,
Rolli Hanspeter,
Jung Marina,
Izdebski Jan
Publication year - 1986
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19860690214
Subject(s) - chemistry , dimer , peptide , intermolecular force , stereochemistry , solubility , histone octamer , molecule , organic chemistry , biochemistry , nucleosome , gene , histone
This study involves L‐lysine oligo peptides, protected at the N‐terminus by the Nps and at the ε‐amino functions by Boc groups. Two series were prepared from dimer to octamer, one containing the p ‐[(cholestan‐3β‐yloxy)carbonyl]benzyl, the other one the benzyl ester group at the C‐terminus. Conformational analyses were performed by IR absorption. The occurrence of the intermolecular β‐structure in the solid state and in CH 2 Cl 2 solution was demonstrated for the highest oligomers. The relative stabilities of the self‐associated species were determined by adding a variety of polar solvents to the CH 2 Cl 2 solutions. The cholestanyl‐containing peptides have a lower propensity to self‐aggregate than the benzyl‐ester analogues. Self‐aggregation and decreasing solubility run in parallel. It was also directly shown that soluble urea derivatives may disrupt intermolecular H‐bonds in CH 2 Cl 2 , a point of practical interest, particularly in solid‐phase peptide synthesis.