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Novel Ester‐Linked Carbohydrate−Peptide Adducts: Effect of the Peptide Substituent on the Pathways of Intramolecular Reactions
Author(s) -
Jeric´ Ivanka,
Horvat Štefica
Publication year - 2001
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/1099-0690(200104)2001:8<1533::aid-ejoc1533>3.0.co;2-y
Subject(s) - chemistry , peptide , intramolecular force , stereochemistry , moiety , substituent , dipeptide , anomer , glycoconjugate , carbohydrate , carbohydrate chemistry , monosaccharide , adduct , biochemistry , organic chemistry
Carbohydrate−peptide conjugates in which D ‐glucose is linked through an ester linkage to the carboxy group of Tyr‐Pro ( 2 ), Tyr‐Pro‐Phe ( 5 ) or Tyr‐Pro‐Phe‐Val ( 11 ), through the C6 hydroxy group of the sugar moiety were synthesized to examine the utility of this type of monosaccharide modification for peptide prodrugs. Evidence is provided that glycoconjugates 2 , 5 , and 11 easily undergo intramolecular chemical transformations, subsequent to attack of the free N ‐terminal amino group at the peptide backbone or at the anomeric position of the D ‐glucose moiety, resulting in the formation of diketopiperazine 12 , glycosylamine 13 , or keto‐sugar derivative 15 . The data indicated that the length and structure of the peptide chain are the main factors that control the intramolecular reactions of the carbohydrate−peptide esters studied.