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Monitoring the Chemical Assembly of a Transmembrane Bradykinin Receptor Fragment: Correlation Between Resin Solvation, Peptide Chain Mobility, and Rate of Coupling
Author(s) -
Oliveira Eliandre,
Cilli Eduardo M.,
Miranda Antonio,
Jubilut Guita N.,
Albericio Fernando,
Andreu David,
Paiva Antonio C. M.,
Schreier Shirley,
Tominaga Mineko,
Nakaie Clovis R.
Publication year - 2002
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(200211)2002:21<3686::aid-ejoc3686>3.0.co;2-5
Subject(s) - chemistry , solvation , peptide , population , stereochemistry , transmembrane protein , solvent , combinatorial chemistry , organic chemistry , receptor , biochemistry , demography , sociology
A combined resin solvation‐peptide chain motion and kinetics of coupling reaction approach was applied to monitor details of the synthesis of TM‐34, a 34‐residue transmembrane segment of the bradykinin receptor. The dynamics of resin‐bound peptide fragments attached to a stable free radical amino acid were examined by EPR spectroscopy. In agreement with an abrupt decrease (from 83 to 43%) in peptide purity occurring in the 12−16 region when DMF was used, a much more strongly immobilized chain population was detected, especially at the 12‐mer stage. Conversely, faster couplings and improved synthesis were observed in 20% DMSO/NMP, probably due to the higher chain mobility in this mixed solvent. In addition, findings relating to solvation of peptide resins seemed to corroborate the previously advanced proposition that the 1:1 sum of electron acceptor and electron donor properties of a solvent can be considered to be an alternative and more appropriate parameter for its polarity. (© Wiley‐VCH Verlag GmbH, 69451 Weinheim, Germany, 2002)